|
Name |
Accession |
Description |
Interval |
E-value |
| CH_CYTSA |
cd21256 |
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma ... |
999-1078 |
1.56e-42 |
|
calponin homology (CH) domain found in cytospin-A; Cytospin-A, also called renal carcinoma antigen NY-REN-22, or sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like protein (SPECC1L), is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-A contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409105 Cd Length: 119 Bit Score: 150.99 E-value: 1.56e-42
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 999 KDPLSALAREYGGSKRNALLKWCQKKTEGYQ---------------------------------------RRNFMLAFQA 1039
Cdd:cd21256 1 KDPLSALAREYGGSKRNALLKWCQKKTEGYQniditnfssswndglafcallhtylpahipyqelnsqdkRRNFTLAFQA 80
|
90 100 110
....*....|....*....|....*....|....*....
gi 1844083964 1040 AESVGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYFET 1078
Cdd:cd21256 81 AESVGIKSTLDINEMVRTERPDWQSVMTYVTAIYKYFET 119
|
|
| CH_CYTS |
cd21199 |
calponin homology (CH) domain found in the cytospin family; The cytospin family includes ... |
1005-1077 |
1.26e-40 |
|
calponin homology (CH) domain found in the cytospin family; The cytospin family includes cytospin-A and cytospin-B. Cytospin-A, also called renal carcinoma antigen NY-REN-22, sperm antigen with calponin homology and coiled-coil domains 1-like, or SPECC1-like (SPECC1L) protein, is involved in cytokinesis and spindle organization. It may play a role in actin cytoskeleton organization and microtubule stabilization and hence, is required for proper cell adhesion and migration. Cytospin-B, also called nuclear structure protein 5 (NSP5), sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion partner to PDGFRB in juvenile myelomonocytic leukemia with translocation t(5;17)(q33;p11.2). Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409048 Cd Length: 112 Bit Score: 145.20 E-value: 1.26e-40
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1005 LAREYGGSKRNALLKWCQKKTEGY---------------------------------------QRRNFMLAFQAAESVGI 1045
Cdd:cd21199 1 LARRYGGSKRNALLKWCQEKTQGYkgiditnfssswndglafcallhsylpdkipyselnpqdKRRNFTLAFKAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 1844083964 1046 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1077
Cdd:cd21199 81 PTTLTIDEMVSMERPDWQSVMSYVTAIYKHFE 112
|
|
| CH_CYTSB |
cd21257 |
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure ... |
1005-1077 |
2.07e-34 |
|
calponin homology (CH) domain found in cytospin-B; Cytospin-B, also called nuclear structure protein 5 (NSP5), or sperm antigen HCMOGT-1, or sperm antigen with calponin homology and coiled-coil domains 1 (SPECC1), is a novel fusion Cytospin-B that contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409106 Cd Length: 112 Bit Score: 127.45 E-value: 2.07e-34
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1005 LAREYGGSKRNALLKWCQKKTEGYQ---------------------------------------RRNFMLAFQAAESVGI 1045
Cdd:cd21257 1 LAREYGGSKRNALLKWCQKKTEGYPniditnfssswsdglafcallhtylpahipyqelssqdkKRNLLLAFQAAESVGI 80
|
90 100 110
....*....|....*....|....*....|..
gi 1844083964 1046 KSTLDINEMVRTERPDWQNVMLYVTAIYKYFE 1077
Cdd:cd21257 81 KPSLELSEMMYTDRPDWQSVMQYVAQIYKYFE 112
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
500-801 |
3.87e-13 |
|
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: 73.94 E-value: 3.87e-13
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 500 ENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRL 579
Cdd:TIGR02168 680 EELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTEL 759
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 580 KAQLENEKQKVAELySIHNSGDKSDIQDLLESVRLDKEKAETL----------ASSLQEDLAHTRNDANRLQDAIAKVED 649
Cdd:TIGR02168 760 EAEIEELEERLEEA-EEELAEAEAEIEELEAQIEQLKEELKALrealdelraeLTLLNEEAANLRERLESLERRIAATER 838
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 650 EYRAFQEEAKK----------QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVK 719
Cdd:TIGR02168 839 RLEDLEEQIEElsedieslaaEIEELEELIEELESELEALLNERASLEEALALLRSELEELSEELRELESKRSELRRELE 918
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 720 KLQDQKHDMEREIKTLHRRLRE-ESAEWRQFQADLQTAVVIANDIKS---EAQEEIGDLKRRLHEAQEKNEKLTKELEEI 795
Cdd:TIGR02168 919 ELREKLAQLELRLEGLEVRIDNlQERLSEEYSLTLEEAEALENKIEDdeeEARRRLKRLENKIKELGPVNLAAIEEYEEL 998
|
....*.
gi 1844083964 796 KSRKQE 801
Cdd:TIGR02168 999 KERYDF 1004
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
528-803 |
1.60e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 71.89 E-value: 1.60e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 528 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdksdiqd 607
Cdd:COG1196 235 RELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQD----------- 303
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 608 lLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMK 687
Cdd:COG1196 304 -IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEE----LEEAEEELEEAEAELAEAEEALLEAEAELAEAE 378
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 688 ETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEA 767
Cdd:COG1196 379 EELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEE 458
|
250 260 270
....*....|....*....|....*....|....*.
gi 1844083964 768 QEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1196 459 EALLELLAELLEEAALLEAALAELLEELAEAAARLL 494
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
604-799 |
1.99e-12 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 71.87 E-value: 1.99e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 604 DIQDLLESVRLDKEKAETLA--SSLQEDLAHTRNDANRLQDAIAKVEDeYRAFQ--EEAKKQIEDLNMTLEKLRSDLDEK 679
Cdd:COG4913 236 DLERAHEALEDAREQIELLEpiRELAERYAAARERLAELEYLRAALRL-WFAQRrlELLEAELEELRAELARLEAELERL 314
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 680 ETERSDMKETIFELEDEVEQHravklhDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLR-------EESAEWRQFQAD 752
Cdd:COG4913 315 EARLDALREELDELEAQIRGN------GGDRLEQLEREIERLERELEERERRRARLEALLAalglplpASAEEFAALRAE 388
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844083964 753 LQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRK 799
Cdd:COG4913 389 AAALLEALEEELEALEEALAEAEAALRDLRRELRELEAEIASLERRK 435
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
202-804 |
3.31e-12 |
|
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: 71.24 E-value: 3.31e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 202 LRNELRDMRAQLGINEDHSEGDEKSEKETI---MAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNALGfSL 278
Cdd:TIGR02168 218 LKAELRELELALLVLRLEELREELEELQEElkeAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALA-NE 296
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 279 EQRLDNSEKLFGYQSLSPEITPGNQSDGGGTLTSSVEGSApgsvEDLLSQDENTLMDHQHSNSMDNLDSECSEVYQPLTS 358
Cdd:TIGR02168 297 ISRLEQQKQILRERLANLERQLEELEAQLEELESKLDELA----EELAELEEKLEELKEELESLEAELEELEAELEELES 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 359 SDDALDAPSSSESEGIPSIER---------SRKGSSGNASEVSVACLTERIHQMEENQHSTseELQATLQELADLQQITQ 429
Cdd:TIGR02168 373 RLEELEEQLETLRSKVAQLELqiaslnneiERLEARLERLEDRRERLQQEIEELLKKLEEA--ELKELQAELEELEEELE 450
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 430 ELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhisyvidedvksgrYMELEQRYMDLAENARF---ER 506
Cdd:TIGR02168 451 ELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDS---------------LERLQENLEGFSEGVKAllkNQ 515
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 507 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGA-----LKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKA 581
Cdd:TIGR02168 516 SGLSGILGVLSELISVDEGYEAAIEAALGGrlqavVVENLNAAKKAIAFLKQNELGRVTFLPLDSIKGTEIQGNDREILK 595
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 582 QLENEKQKVAELYSIHNSGDKSdIQDLLESVR-----------LDKEKAETLASSLQEDLAH------------------ 632
Cdd:TIGR02168 596 NIEGFLGVAKDLVKFDPKLRKA-LSYLLGGVLvvddldnalelAKKLRPGYRIVTLDGDLVRpggvitggsaktnssile 674
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 633 TRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNL 709
Cdd:TIGR02168 675 RRREIEELEEKIEELEEKIAELEkalAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 710 IISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKA----LREALDELRAELTLLNEEAANLRERLESLE 830
|
650
....*....|....*
gi 1844083964 790 KELEEIKSRKQEEER 804
Cdd:TIGR02168 831 RRIAATERRLEDLEE 845
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
505-815 |
8.26e-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: 69.71 E-value: 8.26e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 505 EREQLLGVQQHLSNTLKMAEQDNKEAQEMIG--------------ALKERSHHMERIIESEQKGKAA-------LAATLE 563
Cdd:TIGR02169 689 ELSSLQSELRRIENRLDELSQELSDASRKIGeiekeieqleqeeeKLKERLEELEEDLSSLEQEIENvkselkeLEARIE 768
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 564 EYKATVASDQIEMNRLKA--------QLENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 635
Cdd:TIGR02169 769 ELEEDLHKLEEALNDLEArlshsripEIQAELSKLEEEVS-RIEARLREIEQKLNRLTLEKEYLEKEIQELQEQRIDLKE 847
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 636 DANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavklhdnLIIS 712
Cdd:TIGR02169 848 QIKSIEKEIENLNGKKEELEEELEEleaALRDLESRLGDLKKERDELEAQLRELERKIEELEAQIEKKR-------KRLS 920
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 713 DLENTVKKLQDQkhdmEREIKTLHRRLREESAEW---RQFQADLQ---TAVVIANDIKSEAQEEIGDLKRRLHEAQEKNE 786
Cdd:TIGR02169 921 ELKAKLEALEEE----LSEIEDPKGEDEEIPEEElslEDVQAELQrveEEIRALEPVNMLAIQEYEEVLKRLDELKEKRA 996
|
330 340
....*....|....*....|....*....
gi 1844083964 787 KLTKELEEIKSRKQEEERGRVYNYMNAVE 815
Cdd:TIGR02169 997 KLEEERKAILERIEEYEKKKREVFMEAFE 1025
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
551-804 |
9.89e-12 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 69.58 E-value: 9.89e-12
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 551 EQKGKA----ALAATLEEYKATVASDQIEmnRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSL 626
Cdd:COG1196 207 RQAEKAeryrELKEELKELEAELLLLKLR--ELEAELEELEAELEEL--------EAELEELEAELAELEAELEELRLEL 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 627 QE---DLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAv 703
Cdd:COG1196 277 EElelELEEAQAEEYELLAELARLEQD----IARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEE- 351
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 704 klhdnliisDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQE 783
Cdd:COG1196 352 ---------ELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEE 422
|
250 260
....*....|....*....|.
gi 1844083964 784 KNEKLTKELEEIKSRKQEEER 804
Cdd:COG1196 423 LEELEEALAELEEEEEEEEEA 443
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
567-821 |
1.10e-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: 69.33 E-value: 1.10e-11
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 567 ATVASDQIEMNRLKAQLENEKQKVAELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQE----DLAHTRNDANRLQD 642
Cdd:TIGR02169 163 AGVAEFDRKKEKALEELEEVEENIERLDLIID--EKRQQLERLRREREKAERYQALLKEKREyegyELLKEKEALERQKE 240
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 643 AIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDM--------KETIFELEDEVEQHRAVKLHDNLIISDL 714
Cdd:TIGR02169 241 AIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLgeeeqlrvKEKIGELEAEIASLERSIAEKERELEDA 320
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 715 ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE---EIGDLKRRLHEAQEKNEKLTKE 791
Cdd:TIGR02169 321 EERLAKLEAEIDKLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEvdkEFAETRDELKDYREKLEKLKRE 400
|
250 260 270
....*....|....*....|....*....|....*....
gi 1844083964 792 LEEIK---------SRKQEEERGRVYNYMNAVERDLAAL 821
Cdd:TIGR02169 401 INELKreldrlqeeLQRLSEELADLNAAIAGIEAKINEL 439
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
396-803 |
3.21e-10 |
|
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: 64.69 E-value: 3.21e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmeslcqqsdklehfSRQIeyfrslldehhi 475
Cdd:TIGR02168 682 LEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEEL---------------------SRQI------------ 728
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 476 syvidedvkSGRYMELEQrymdlaenARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKershhmERIIESEQKgK 555
Cdd:TIGR02168 729 ---------SALRKDLAR--------LEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAE------EELAEAEAE-I 784
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 556 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS--GDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:TIGR02168 785 EELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESleRRIAATERRLEDLEEQIEELSEDIESLAAEIEEL 864
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 634 RNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQhraVKLHDNLIISD 713
Cdd:TIGR02168 865 EELIEELESELEALLNERASLEEALALLRSE----LEELSEELRELESKRSELRRELEELREKLAQ---LELRLEGLEVR 937
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 714 LENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLheaqeknEKLTKELE 793
Cdd:TIGR02168 938 IDNLQERLSEEYSLTLEEAEALENKIEDDEEEARRRLKRLENKIKELGPVNLAAIEEYEELKERY-------DFLTAQKE 1010
|
410
....*....|.
gi 1844083964 794 EI-KSRKQEEE 803
Cdd:TIGR02168 1011 DLtEAKETLEE 1021
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
529-804 |
7.99e-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: 63.16 E-value: 7.99e-10
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 529 EAQEMIGALK-ERSHHMERIIESEQKGKAALAAtLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSihnsgDKSDIQD 607
Cdd:TIGR02169 678 RLRERLEGLKrELSSLQSELRRIENRLDELSQE-LSDASRKIGEIEKEIEQLEQEEEKLKERLEELEE-----DLSSLEQ 751
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 608 LLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIA-----KVEDEYRAFQEEAKKQ----------IEDLNMTLEKL 672
Cdd:TIGR02169 752 EIENVKSELKELEARIEELEEDLHKLEEALNDLEARLShsripEIQAELSKLEEEVSRIearlreieqkLNRLTLEKEYL 831
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 673 RSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQAD 752
Cdd:TIGR02169 832 EKEIQELQEQRIDLKEQIKSIEKEIENLNGKKEELEEELEELEAALRDLESRLGDLKKERDELEAQLRELERKIEELEAQ 911
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 753 LQTAVVIANDIK---SEAQEEIGDLKRRLHEAQEKNEKlTKELEEIKSRKQEEER 804
Cdd:TIGR02169 912 IEKKRKRLSELKaklEALEEELSEIEDPKGEDEEIPEE-ELSLEDVQAELQRVEE 965
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
398-825 |
1.08e-09 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 62.77 E-value: 1.08e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 398 ERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHhiSY 477
Cdd:PRK03918 207 REINEISSELPELREELEKLEKEVKELEELKEEIEELEKEL--------ESLEGSKRKLEEKIRELEERIEELKKE--IE 276
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 478 VIDEDVKSGRYME-LEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESE---QK 553
Cdd:PRK03918 277 ELEEKVKELKELKeKAEEYIKLSE----FYEEYLDELREIEKRLSRLEEEINGIEERIKELEEKEERLEELKKKLkelEK 352
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 554 GKAALAATLEEYKatvasdqiEMNRLKAQLENEKQKVAELysihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:PRK03918 353 RLEELEERHELYE--------EAKAKKEELERLKKRLTGL-------TPEKLEKELEELEKAKEEIEEEISKITARIGEL 417
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 634 RNDANRLQDAIAKVE----------------------DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERS------- 684
Cdd:PRK03918 418 KKEIKELKKAIEELKkakgkcpvcgrelteehrkellEEYTAELKRIEKELKEIEEKERKLRKELRELEKVLKkeselik 497
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 685 --DMKETIFELEDEVEQH-----------------RAVKLHDNLI--------ISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:PRK03918 498 lkELAEQLKELEEKLKKYnleelekkaeeyeklkeKLIKLKGEIKslkkelekLEELKKKLAELEKKLDELEEELAELLK 577
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 738 RLREES-----------AEWRQFQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEK-------NEKLTKELEEIKSRK 799
Cdd:PRK03918 578 ELEELGfesveeleerlKELEPFYNEYLELKDAEKELERE-EKELKKLEEELDKAFEElaetekrLEELRKELEELEKKY 656
|
490 500
....*....|....*....|....*.
gi 1844083964 800 QEEERGRVYNYMNAVERDLAALRQGM 825
Cdd:PRK03918 657 SEEEYEELREEYLELSRELAGLRAEL 682
|
|
| CH_ACTN_rpt2 |
cd21216 |
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin ... |
1012-1076 |
1.21e-09 |
|
second calponin homology (CH) domain found in the alpha-actinin family; The alpha-actinin (ACTN) family includes alpha-actinin-1, -2, -3, and -4. They are F-actin cross-linking proteins which are thought to anchor actin to a variety of intracellular structures. ACTN1 mutations cause congenital macrothrombocytopenia. ACTN2 mutations are associated with cardiomyopathies, as well as skeletal muscle disorder. ACTN3 is critical in anchoring the myofibrillar actin filaments and plays a key role in muscle contraction. ACTN4 is associated with cell motility and cancer invasion. It is probably involved in vesicular trafficking via its association with the CART complex, which is necessary for efficient transferrin receptor recycling but not for epidermal growth factor receptor (EGFR) degradation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409065 Cd Length: 115 Bit Score: 56.99 E-value: 1.21e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1012 SKRNALLKWCQKKTEGYQ---------------------------------------RRNFMLAFQAAE-SVGIKSTLDI 1051
Cdd:cd21216 10 SAKEGLLLWCQRKTAPYKnvnvqnfhtswkdglafcalihrhrpdlldydklrkddpRENLNLAFDVAEkHLDIPKMLDA 89
|
90 100
....*....|....*....|....*
gi 1844083964 1052 NEMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21216 90 EDIVNTPRPDERSVMTYVSCYYHAF 114
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
613-823 |
1.22e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 62.65 E-value: 1.22e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 613 RLDKEKAETLasslqEDLAHTRNDANRLQDAIAKVED-------------EYRAFQEEAKK--------QIEDLNMTLEK 671
Cdd:COG1196 169 KYKERKEEAE-----RKLEATEENLERLEDILGELERqleplerqaekaeRYRELKEELKEleaellllKLRELEAELEE 243
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 672 LRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQA 751
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEE 323
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|..
gi 1844083964 752 DLQTavviANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALRQ 823
Cdd:COG1196 324 ELAE----LEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAEL-----AEAEEELEELAE 386
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
396-822 |
1.66e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 61.98 E-value: 1.66e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDehhi 475
Cdd:PRK02224 326 LRDRLEECRVAAQAHNEEAESLREDADDLEERAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFG---- 401
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 476 syviDEDVKSGrymELEQRYMDLAEnarfEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALK--------ERSHHMERI 547
Cdd:PRK02224 402 ----DAPVDLG---NAEDFLEELRE----ERDELREREAELEATLRTARERVEEAEALLEAGKcpecgqpvEGSPHVETI 470
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 548 IESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaelysihnsgdksdiqdlLESVRLDKEKAETLASSLQ 627
Cdd:PRK02224 471 EEDRER-VEELEAELEDLEEEVEEVEERLERAEDLVEAEDR--------------------IERLEERREDLEELIAERR 529
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 628 EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLnmtlEKLRSDLDEKETERSDMKETIFELEDEVEQHRAvklhd 707
Cdd:PRK02224 530 ETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEA----EEAREEVAELNSKLAELKERIESLERIRTLLAA----- 600
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 708 nliISDLENTVKKLQDQKHDMErEIKTLHR-RLREESAEWRQFQADLQTAvviandikseaqeeigdlkrRLHEAQEKNE 786
Cdd:PRK02224 601 ---IADAEDEIERLREKREALA-ELNDERReRLAEKRERKRELEAEFDEA--------------------RIEEAREDKE 656
|
410 420 430
....*....|....*....|....*....|....*...
gi 1844083964 787 KLTKELEEI--KSRKQEEERGRVYNYMNAVERDLAALR 822
Cdd:PRK02224 657 RAEEYLEQVeeKLDELREERDDLQAEIGAVENELEELE 694
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
609-804 |
1.99e-09 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 61.88 E-value: 1.99e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 609 LESVRLDKEKAE---TLASSLQE--------DLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLD 677
Cdd:COG1196 202 LEPLERQAEKAEryrELKEELKEleaellllKLRELEAELEELEAELEELEAE----LEELEAELAELEAELEELRLELE 277
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 678 EKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG1196 278 ELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAE 357
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844083964 758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG1196 358 AELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAELAAQLEE 404
|
|
| COG2433 |
COG2433 |
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only]; |
669-806 |
2.11e-09 |
|
Possible nuclease of RNase H fold, RuvC/YqgF family [General function prediction only];
Pssm-ID: 441980 [Multi-domain] Cd Length: 644 Bit Score: 61.41 E-value: 2.11e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 669 LEKLRSDLDEKETERSDMKETIFELEDEVEQHRavklhdnliISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQ 748
Cdd:COG2433 382 LEELIEKELPEEEPEAEREKEHEERELTEEEEE---------IRRLEEQVERLEAEVEELEAELEEKDERIERLERELSE 452
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083964 749 FQADLQTAVVIANDIKSEaQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:COG2433 453 ARSEERREIRKDREISRL-DREIERLERELEEERERIEELKRKLERLKELWKLEHSGE 509
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
387-797 |
3.72e-09 |
|
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: 60.80 E-value: 3.72e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVIL---MESLCQQSDKLEHFSRQI 463
Cdd:TIGR04523 120 NKLEVELNKLEKQKKENKKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENELNLLekeKLNIQKNIDKIKNKLLKL 199
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 464 EYFRSLLDehhiSYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHH 543
Cdd:TIGR04523 200 ELLLSNLK----KKIQKNKSLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKE 275
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 544 MERI---IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYS-IHNSGDK-SDIQDLLESVRLDKEK 618
Cdd:TIGR04523 276 LEQNnkkIKELEKQLNQLKSEISDLNNQKEQDW--NKELKSELKNQEKKLEEIQNqISQNNKIiSQLNEQISQLKKELTN 353
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 619 AETLASSLQEDLahtrndaNRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELED 695
Cdd:TIGR04523 354 SESENSEKQREL-------EEKQNEIEKLKKENQSYKQEIKNlesQINDLESKIQNQEKLNQQKDEQIKKLQQEKELLEK 426
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 696 EVEQHRAVKLHDNLIISDLEN-------TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQ 768
Cdd:TIGR04523 427 EIERLKETIIKNNSEIKDLTNqdsvkelIIKNLDNTRESLETQLKVLSRSINKIKQNLEQKQKELKSKEKELKKLNEEKK 506
|
410 420 430
....*....|....*....|....*....|..
gi 1844083964 769 ---EEIGDLKRRLHEAQEKNEKLTKELEEIKS 797
Cdd:TIGR04523 507 eleEKVKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
412-824 |
4.10e-09 |
|
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: 60.85 E-value: 4.10e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 412 EELQATLQELADLQQITQELNSENERLGEEKvilmeslcqqsdklehfsRQIEYFRSLLDEHhisyvidEDVksgRYMEL 491
Cdd:TIGR02169 177 EELEEVEENIERLDLIIDEKRQQLERLRRER------------------EKAERYQALLKEK-------REY---EGYEL 228
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 492 EQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQkgkAALAATLEEYKATVAS 571
Cdd:TIGR02169 229 LKEKEALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQ---LRVKEKIGELEAEIAS 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 572 --DQIEMNRLKAQ-LENEKQKVAELYSiHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVE 648
Cdd:TIGR02169 306 leRSIAEKERELEdAEERLAKLEAEID-KLLAEIEELEREIEEERKRRDKLTEEYAELKEELEDLRAELEEVDKEFAETR 384
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 649 DEYRAFQEEakkqiedlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDM 728
Cdd:TIGR02169 385 DELKDYREK-----------LEKLKREINELKRELDRLQEELQRLSEELADLNAA-------IAGIEAKINELEEEKEDK 446
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 729 EREIKTLHRRLREESAewrqfqadlqtavviandIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVY 808
Cdd:TIGR02169 447 ALEIKKQEWKLEQLAA------------------DLSKYEQELYDLKEEYDRVEKELSKLQRELAEAEAQARASEERVRG 508
|
410
....*....|....*.
gi 1844083964 809 NYmnAVERDLAALRQG 824
Cdd:TIGR02169 509 GR--AVEEVLKASIQG 522
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
387-822 |
6.25e-09 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 60.05 E-value: 6.25e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 387 NASEVSVACLTERIHQMEENQhstsEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYF 466
Cdd:PRK02224 209 NGLESELAELDEEIERYEEQR----EQARETRDEADEVLEEHEERREELETLEAEIEDLRETIAETEREREELAEEVRDL 284
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 467 RSLLDEHhisyvidEDVKSGRYMELEQRYMDlAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMER 546
Cdd:PRK02224 285 RERLEEL-------EEERDDLLAEAGLDDAD-AEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 547 IIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSL 626
Cdd:PRK02224 357 RAEELREEAAELESELEEAREAVEDRREEIEELEEEIEELRERFGDA-----PVDLGNAEDFLEELREERDELREREAEL 431
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 627 QEDLAHTRND---ANRLQDA--------------IAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLD------EKETER 683
Cdd:PRK02224 432 EATLRTARERveeAEALLEAgkcpecgqpvegspHVETIEEDRERVEELEAELEDLEEEVEEVEERLEraedlvEAEDRI 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 684 SDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQADLQTAVVIA 760
Cdd:PRK02224 512 ERLEERREDLEELIAERRETIEEKRERAEELRERAAELEAEAEEKREAAAEAEEEaeeAREEVAELNSKLAELKERIESL 591
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 761 NDIKS------EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE--------------EERGRVYNYMNAVERDLAA 820
Cdd:PRK02224 592 ERIRTllaaiaDAEDEIERLREKREALAELNDERRERLAEKRERKREleaefdearieearEDKERAEEYLEQVEEKLDE 671
|
..
gi 1844083964 821 LR 822
Cdd:PRK02224 672 LR 673
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
630-829 |
7.77e-09 |
|
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: 60.07 E-value: 7.77e-09
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 630 LAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---------------------QIEDLNMTLEKLRSDLDEKETERSDMKE 688
Cdd:TIGR02168 181 LERTRENLDRLEDILNELERQLKSLERQAEKaerykelkaelrelelallvlRLEELREELEELQEELKEAEEELEELTA 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 689 TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTA---VVIANDIKS 765
Cdd:TIGR02168 261 ELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEELeskLDELAEELA 340
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083964 766 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGrvynyMNAVERDLAALRQGMGLSR 829
Cdd:TIGR02168 341 ELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ-----LETLRSKVAQLELQIASLN 399
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
405-803 |
2.20e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 58.53 E-value: 2.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 405 ENQHSTSEELQATLQELADLQQITQELNSEnerlgeekvilMESLCQQSDKLEHFsrqIEYfRSLLDEHHISYVIDedvk 484
Cdd:TIGR02168 172 ERRKETERKLERTRENLDRLEDILNELERQ-----------LKSLERQAEKAERY---KEL-KAELRELELALLVL---- 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 485 sgRYMELEQRYmdlaENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEE 564
Cdd:TIGR02168 233 --RLEELREEL----EELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQI 306
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 565 YKATVASDQIEMNRLKAQLENEKQKvaelysihnsgdksdiqdllesvrldKEKAETLASSLQEDLAHTRNDANRLQDAI 644
Cdd:TIGR02168 307 LRERLANLERQLEELEAQLEELESK--------------------------LDELAEELAELEEKLEELKEELESLEAEL 360
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 645 akveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQhravklhdnliisdLENTVKKLQDQ 724
Cdd:TIGR02168 361 ----EELEAELEELESRLEELEEQLETLRSKVAQLELQIASLNNEIERLEARLER--------------LEDRRERLQQE 422
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 725 KHDMEREIKTLHRR-LREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:TIGR02168 423 IEELLKKLEEAELKeLQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQARLDSLERLQENLE 502
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
412-808 |
2.21e-08 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 58.24 E-value: 2.21e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 412 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEdvKSGRYMEL 491
Cdd:COG4717 74 KELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQLLPLYQELEALEAELAE--LPERLEEL 151
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 492 EQRYMDLAEnARFEREQLLGVQQHLSNTLKMAEQDNKEA--QEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATV 569
Cdd:COG4717 152 EERLEELRE-LEEELEELEAELAELQEELEELLEQLSLAteEELQDLAEELEELQQRLAELEEE-LEEAQEELEELEEEL 229
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 570 asDQIEMNRLKAQLENEKQKVAELYSIHN-----SGDKSDIQDLLESV--------------RLDKEKAETLASSLQEDL 630
Cdd:COG4717 230 --EQLENELEAAALEERLKEARLLLLIAAallalLGLGGSLLSLILTIagvlflvlgllallFLLLAREKASLGKEAEEL 307
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 631 AHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSdmketifELEDEVEQHRAVKLHDNLI 710
Cdd:COG4717 308 QALPALEELEEEELEELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEE-------ELQLEELEQEIAALLAEAG 380
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 711 ISDLENTVKKLQ--DQKHDMEREIKTLHRRLREESAEWRQFQADLQtavviandiKSEAQEEIGDLKRRLHEAQEKNEKL 788
Cdd:COG4717 381 VEDEEELRAALEqaEEYQELKEELEELEEQLEELLGELEELLEALD---------EEELEEELEELEEELEELEEELEEL 451
|
410 420
....*....|....*....|
gi 1844083964 789 TKELEEIKSRKQEEERGRVY 808
Cdd:COG4717 452 REELAELEAELEQLEEDGEL 471
|
|
| CH_SMTN-like |
cd21200 |
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes ... |
1014-1076 |
3.20e-08 |
|
calponin homology (CH) domain found in the smoothelin family; The smoothelin family includes smoothelin and smoothelin-like proteins. Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. SMTNL1, also called calponin homology-associated smooth muscle protein (CHASM), plays a role in the regulation of contractile properties of both striated and smooth muscles. It can bind to calmodulin and tropomyosin. When it is unphosphorylated, SMTNL1 may inhibit myosin dephosphorylation. SMTNL2 is highly expressed in skeletal muscle and could be associated with differentiating myocytes. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409049 Cd Length: 107 Bit Score: 52.73 E-value: 3.20e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1014 RNALLKWCQKKTEGYQ---------------------------------------RRNFMLAFQAAES-VGIKSTLDINE 1053
Cdd:cd21200 3 KQMLLEWCQAKTRGYEhvditnfssswsdgmafcalihhffpdafdyssldpknrRKNFELAFSTAEElADIAPLLEVED 82
|
90 100
....*....|....*....|....
gi 1844083964 1054 MVRTE-RPDWQNVMLYVTAIYKYF 1076
Cdd:cd21200 83 MVRMGnRPDWKCVFTYVQSLYRHL 106
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
575-823 |
3.67e-08 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 57.76 E-value: 3.67e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKAQLENEKQKVAELYSIHNSGD--KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAkvedEYR 652
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTaeLQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQ----ILR 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 653 AFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEV---------------EQHRAVKLHDNLI------I 711
Cdd:TIGR02168 309 ERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELesleaeleeleaeleELESRLEELEEQLetlrskV 388
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 712 SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKE 791
Cdd:TIGR02168 389 AQLELQIASLNNEIERLEARLERLEDRRERLQQEIEELLKKLEEAE------LKELQAELEELEEELEELQEELERLEEA 462
|
250 260 270
....*....|....*....|....*....|..
gi 1844083964 792 LEEIKSRKQEEERGRVynymnAVERDLAALRQ 823
Cdd:TIGR02168 463 LEELREELEEAEQALD-----AAERELAQLQA 489
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
387-699 |
3.75e-08 |
|
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: 57.77 E-value: 3.75e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 387 NASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESlcqqsdKLEHFSRQIEYF 466
Cdd:TIGR02169 233 EALERQKEAIERQLASLEEELEKLTEEISELEKRLEEIEQLLEELNKKIKDLGEEEQLRVKE------KIGELEAEIASL 306
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 467 RSLLDehhisyvidedvksgrymELEQRYMDLAENARfereqllgvqqhlsntlkmaeqdnkEAQEMIGALKERSHHMER 546
Cdd:TIGR02169 307 ERSIA------------------EKERELEDAEERLA-------------------------KLEAEIDKLLAEIEELER 343
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 547 IIESEQKGKAALaatleeyKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDK--SDIQDLLESVRLDKEKAETLAS 624
Cdd:TIGR02169 344 EIEEERKRRDKL-------TEEYAELKEELEDLRAELEEVDKEFAETRDELKDYREklEKLKREINELKRELDRLQEELQ 416
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 625 SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtLEKLRSDLDEKETERSDMKETIFELEDEVEQ 699
Cdd:TIGR02169 417 RLSEELADLNAAIAGIEAKINELEEEKEDKALEIKKQEWK----LEQLAADLSKYEQELYDLKEEYDRVEKELSK 487
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
620-823 |
5.02e-08 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 57.36 E-value: 5.02e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 620 ETLASSLQEDLAH---TRNDANRLQDAIAKVEDEYRAFQEEakkqIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDE 696
Cdd:PRK02224 212 ESELAELDEEIERyeeQREQARETRDEADEVLEEHEERREE----LETLEAEIEDLRETIAETEREREELAEEVRDLRER 287
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 697 VEQHRAvKLHDNLIISDLEN-TVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQE------ 769
Cdd:PRK02224 288 LEELEE-ERDDLLAEAGLDDaDAEAVEARREELEDRDEELRDRLEECRVAAQAHNEEAESLREDADDLEERAEElreeaa 366
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 770 ----EIGDLKRRLHEAQEKNEKLTKELEEIKSR--KQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:PRK02224 367 elesELEEAREAVEDRREEIEELEEEIEELRERfgDAPVDLGNAEDFLEELREERDELRE 426
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
390-816 |
5.15e-08 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 57.38 E-value: 5.15e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 390 EVSVACLTERIHQMEENQHSTSEELQATLQELADLQQItQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSL 469
Cdd:PRK03918 251 EGSKRKLEEKIRELEERIEELKKEIEELEEKVKELKEL-KEKAEEYIKLSEFYEEYLDELREIEKRLSRLEEEINGIEER 329
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 470 LDEhhisyvIDEDVK-----SGRYMELEQRYMDLAENAR-FEREQLLGVQ-------------QHLSNTLKMAEQDNKEA 530
Cdd:PRK03918 330 IKE------LEEKEErleelKKKLKELEKRLEELEERHElYEEAKAKKEElerlkkrltgltpEKLEKELEELEKAKEEI 403
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 531 QEMIGALKERSHHMERIIESEQKGKAAL-------------------AATLEEYKATVASDQIEMNRLKAQLENEKQKVA 591
Cdd:PRK03918 404 EEEISKITARIGELKKEIKELKKAIEELkkakgkcpvcgrelteehrKELLEEYTAELKRIEKELKEIEEKERKLRKELR 483
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 592 ELYSIHNsgDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKqIEDLNMTLEK 671
Cdd:PRK03918 484 ELEKVLK--KESELIKLKELAEQLKELEEKLKKYNLEELEKKAEEYEKLKEKLIKLKGEIKSLKKELEK-LEELKKKLAE 560
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 672 LRSDLDEKETERSDMKETI----FELEDEVEQ---------HRAVKLHDnlIISDLENTVKKLQDQKHDMEREIKTL--- 735
Cdd:PRK03918 561 LEKKLDELEEELAELLKELeelgFESVEELEErlkelepfyNEYLELKD--AEKELEREEKELKKLEEELDKAFEELaet 638
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 736 ----------------------HRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLtkELE 793
Cdd:PRK03918 639 ekrleelrkeleelekkyseeeYEELREEYLELSRELAGLRAELEELEKRREEIKKTLEKLKEELEEREKAKKEL--EKL 716
|
490 500
....*....|....*....|...
gi 1844083964 794 EIKSRKQEEERGRVYNYMNAVER 816
Cdd:PRK03918 717 EKALERVEELREKVKKYKALLKE 739
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
399-778 |
5.69e-08 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 57.25 E-value: 5.69e-08
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 399 RIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLgeekvilmeslcqqsdKLEHFSRQIEYfrslldehhisyv 478
Cdd:COG1196 233 KLRELEAELEELEAELEELEAELEELEAELAELEAELEEL----------------RLELEELELEL------------- 283
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 479 ideDVKSGRYMELEQRYMDLAENARFEREQLlgvqQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAAL 558
Cdd:COG1196 284 ---EEAQAEEYELLAELARLEQDIARLEERR----RELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEA 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 559 AATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAN 638
Cdd:COG1196 357 EAELAEAEEALLEAEAELAEAEEELEELAEELLEA-----------LRAAAELAAQLEELEEAEEALLERLERLEEELEE 425
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 639 RLQDAIA--KVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE- 715
Cdd:COG1196 426 LEEALAEleEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEg 505
|
330 340 350 360 370 380
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 716 -NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVV-IANDIKSEAQEEIGDLKRRL 778
Cdd:COG1196 506 fLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAALEAALAAALQnIVVEDDEVAAAAIEYLKAAK 570
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
649-803 |
1.27e-07 |
|
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: 53.78 E-value: 1.27e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 649 DEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQK--H 726
Cdd:COG1579 20 DRLEHRLKELPAELAELEDELAALEARLEAAKTELEDLEKEIKRLELEIEEVEAR-------IKKYEEQLGNVRNNKeyE 92
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083964 727 DMEREIKTLHRRlreesaewrqfQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG1579 93 ALQKEIESLKRR-----------ISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAEL 158
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
397-802 |
3.72e-07 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 54.39 E-value: 3.72e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 397 TERIHQMEENQHSTSEELQATLQELADLQQITQELN--SENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhh 474
Cdd:COG4717 87 EEEYAELQEELEELEEELEELEAELEELREELEKLEklLQLLPLYQELEALEAELAELPERLEELEERLEELRELEEE-- 164
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 475 iSYVIDEDVKSGRYmELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKG 554
Cdd:COG4717 165 -LEELEAELAELQE-ELEELLEQLSLATEEELQDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAALE 242
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 555 K-----------AALAATLEEYKATVASDQIE------------------MNRLKAQLENEKQKVAELYSIHNsGDKSDI 605
Cdd:COG4717 243 ErlkearlllliAAALLALLGLGGSLLSLILTiagvlflvlgllallfllLAREKASLGKEAEELQALPALEE-LEEEEL 321
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 606 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSD 685
Cdd:COG4717 322 EELLAALGLPPDLSPEELLELLDRIEELQELLREAEELEEELQLE--ELEQEIAALLAEAGVEDEEELRAALEQAEEYQE 399
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 686 MKETIFELEDEVEQHR--AVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADlqtavvianDI 763
Cdd:COG4717 400 LKEELEELEEQLEELLgeLEELLEALDEEELEEELEELEEELEELEEELEELREELAELEAELEQLEED---------GE 470
|
410 420 430 440
....*....|....*....|....*....|....*....|....*.
gi 1844083964 764 KSEAQEEIGDLKRRLHEAQEKN-------EKLTKELEEIKSRKQEE 802
Cdd:COG4717 471 LAELLQELEELKAELRELAEEWaalklalELLEEAREEYREERLPP 516
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
575-809 |
5.31e-07 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 53.48 E-value: 5.31e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKaqleneKQKVAELYSihnsgdksDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI---AKVEDEY 651
Cdd:PHA02562 167 EMDKLN------KDKIRELNQ--------QIQTLDMKIDHIQQQIKTYNKNIEEQRKKNGENIARKQNKYdelVEEAKTI 232
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 652 RAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR----------AVKLHDNLI------ISDLE 715
Cdd:PHA02562 233 KAEIEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIEQFQKVIKMYEkggvcptctqQISEGPDRItkikdkLKELQ 312
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 716 NTVKKLQDQKHDMER---EIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSE---AQEEIGDLKRRLHEAQEKNEKLT 789
Cdd:PHA02562 313 HSLEKLDTAIDELEEimdEFNEQSKKLLELKNKISTNKQSLITLVDKAKKVKAAieeLQAEFVDNAEELAKLQDELDKIV 392
|
250 260
....*....|....*....|
gi 1844083964 790 KELEEIKsrKQEEERGRVYN 809
Cdd:PHA02562 393 KTKSELV--KEKYHRGIVTD 410
|
|
| CH_beta_spectrin_rpt2 |
cd21194 |
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin ... |
1012-1076 |
5.93e-07 |
|
second calponin homology (CH) domain found in the beta spectrin family; The beta spectrin family includes beta-I, -II, -III, -IV and -V spectrins. Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. Beta-I spectrin, also called spectrin beta chain, erythrocytic (SPTB), may be involved in anaemia pathogenesis. Beta-II spectrin, also called spectrin beta chain, non-erythrocytic 1 (SPTBN1), or fodrin beta chain, is a component of fodrin, which is the general spectrin-like protein that seems to be involved in secretion. Fodrin interacts with calmodulin in a calcium-dependent manner and is thus a candidate for the calcium-dependent movement of the cytoskeleton at the membrane. Beta-IV spectrin is also called spectrin, non-erythroid beta chain 3 (SPTBN3) or spectrin beta chain, non-erythrocytic 4 (SPTBN4). Its mutation associates with congenital myopathy, neuropathy, and central deafness. Beta-III spectrin is also called spectrin beta chain, non-erythrocytic 2 (SPTBN2), or spinocerebellar ataxia 5 protein (SCA5). Beta-V spectrin, also called spectrin beta chain, non-erythrocytic 5 (SPTBN5), is a mammalian ortholog of Drosophila beta H spectrin. Beta-III and Beta-V spectrins may play crucial roles as longer actin-membrane cross-linkers or fulfill the need for greater extensible flexibility than can be provided by the other smaller conventional spectrins. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409043 Cd Length: 105 Bit Score: 48.95 E-value: 5.93e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1012 SKRNALLKWCQKKTEGYQR---RNFM------LAFQ-------------------------------AAESVGIKSTLDi 1051
Cdd:cd21194 2 SAKDALLLWCQRKTAGYPGvniQNFTtswrdgLAFNalihahrpdlidynrldpndhlgnlnnafdvAEQELGIAKLLD- 80
|
90 100
....*....|....*....|....*
gi 1844083964 1052 NEMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21194 81 AEDVDVARPDEKSIMTYVASYYHYF 105
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
521-804 |
8.52e-07 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 53.61 E-value: 8.52e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 521 KMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATvASDQIEMNRLKAQLENEKQKVAELYSIHNSG 600
Cdd:PTZ00121 1431 KKADEAKKKAEEAKKADEAKKKAEEAKKAEEAKKKAEEAKKADEAKKK-AEEAKKADEAKKKAEEAKKKADEAKKAAEAK 1509
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 601 DKSDIQDLLESVRLDKE--KAETLASSLQEDLAHTRNDANRLQDA--IAKVEDEYRAfqEEAKKQIEDLNMTLEKLRsDL 676
Cdd:PTZ00121 1510 KKADEAKKAEEAKKADEakKAEEAKKADEAKKAEEKKKADELKKAeeLKKAEEKKKA--EEAKKAEEDKNMALRKAE-EA 1586
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 677 DEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDL---ENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADL 753
Cdd:PTZ00121 1587 KKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEElkkAEEEKKKVEQLKKKEAEEKKKAEELKKAEEENKIKAAEE 1666
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|.
gi 1844083964 754 QTAVVIANDIKSEAQEEIGDlKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:PTZ00121 1667 AKKAEEDKKKAEEAKKAEED-EKKAAEALKKEAEEAKKAEELKKKEAEEKK 1716
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
399-696 |
9.47e-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: 53.15 E-value: 9.47e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 399 RIHQMEENQHSTSEE-------LQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL-EHFSRQIEYFRSLL 470
Cdd:TIGR02169 724 EIEQLEQEEEKLKERleeleedLSSLEQEIENVKSELKELEARIEELEEDLHKLEEALNDLEARLsHSRIPEIQAELSKL 803
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 471 DEHHISYvidedvkSGRYMELEQRymdlaENARFEREQLLgvqqhlsntlkmaEQDNKEAQEMIGALKERSHHMERIIES 550
Cdd:TIGR02169 804 EEEVSRI-------EARLREIEQK-----LNRLTLEKEYL-------------EKEIQELQEQRIDLKEQIKSIEKEIEN 858
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 551 EQKGKAALAATLEEYKATV-------ASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLA 623
Cdd:TIGR02169 859 LNGKKEELEEELEELEAALrdlesrlGDLKKERDELEAQLRELERKIEEL--------EAQIEKKRKRLSELKAKLEALE 930
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 624 SSLQEDLAHTRND---------ANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLrSDLDEK----ETERSDMKETI 690
Cdd:TIGR02169 931 EELSEIEDPKGEDeeipeeelsLEDVQAELQRVEEEIRALEPVNMLAIQEYEEVLKRL-DELKEKraklEEERKAILERI 1009
|
....*.
gi 1844083964 691 FELEDE 696
Cdd:TIGR02169 1010 EEYEKK 1015
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
396-801 |
1.26e-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: 1.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLE------------------ 457
Cdd:pfam05483 273 LEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSMSTQKALEEDLQIATKTICQLTEEKEaqmeelnkakaahsfvvt 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 458 HFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARF---------EREQLLGVQQHL----SNTLKMAE 524
Cdd:pfam05483 353 EFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFknnkeveleELKKILAEDEKLldekKQFEKIAE 432
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 525 QDNKEAQEMIGALKERSHHMERIieseqKGKAALAATLEEYKATvasdqiEMNRLKAQLENEKQKVAELYSIHNsgdksd 604
Cdd:pfam05483 433 ELKGKEQELIFLLQAREKEIHDL-----EIQLTAIKTSEEHYLK------EVEDLKTELEKEKLKNIELTAHCD------ 495
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 605 iQDLLESVRLDKEKAETLAS--SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKEte 682
Cdd:pfam05483 496 -KLLLENKELTQEASDMTLElkKHQEDIINCKKQEERMLKQIENLEEKEMNLRDELESVREEFIQKGDEVKCKLDKSE-- 572
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 683 rSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDqkhdMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:pfam05483 573 -ENARSIEYEVLKKEKQMKILENKCNNLKKQIENKNKNIEE----LHQENKALKKKGSAENKQLNAYEIKVNKLELELAS 647
|
410 420 430
....*....|....*....|....*....|....*....
gi 1844083964 763 IKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam05483 648 AKQKFEEIIDNYQKEIEDKKISEEKLLEEVEKAKAIADE 686
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
499-764 |
1.28e-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: 52.07 E-value: 1.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 499 AENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKErshhMERIIESEQKGKAALAATLEEYKATVASDQIEMNR 578
Cdd:COG4942 19 ADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAA----LERRIAALARRIRALEQELAALEAELAELEKEIAE 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 579 LKAQLENEKQKVAE-LYSIHNSGDKSDIQDLLEsvrldkekaetlasslQEDLahtrNDANRLQDAiakvedeYRAFQEE 657
Cdd:COG4942 95 LRAELEAQKEELAElLRALYRLGRQPPLALLLS----------------PEDF----LDAVRRLQY-------LKYLAPA 147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 658 AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:COG4942 148 RREQAEELRADLAELAALRAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEA 227
|
250 260
....*....|....*....|....*..
gi 1844083964 738 RLREESAEWRQFQADLQTAVVIANDIK 764
Cdd:COG4942 228 LIARLEAEAAAAAERTPAAGFAALKGK 254
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
602-803 |
1.60e-06 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 52.08 E-value: 1.60e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 602 KSDIQDLLESVRLDK--EKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEeAKKQIEDLNMTLEKLRSDLDEK 679
Cdd:COG4717 36 KSTLLAFIRAMLLERleKEADELFKPQGRKPELNLKELKELEEELKEAEEKEEEYAE-LQEELEELEEELEELEAELEEL 114
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 680 ETERSDMKETI--FELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG4717 115 REELEKLEKLLqlLPLYQELEALEAELAELPERLEELEERLEELRELEEELEELEAELAELQEELEELLEQLSLATEEEL 194
|
170 180 190 200
....*....|....*....|....*....|....*....|....*.
gi 1844083964 758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:COG4717 195 QDLAEELEELQQRLAELEEELEEAQEELEELEEELEQLENELEAAA 240
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
619-895 |
1.75e-06 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 51.37 E-value: 1.75e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 619 AETLASSLQEDLAHTRNDANRLQDAIAKVEDEYrafqEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVE 698
Cdd:COG3883 14 ADPQIQAKQKELSELQAELEAAQAELDALQAEL----EELNEEYNELQAELEALQAEIDKLQAEIAEAEAEIEERREELG 89
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 699 QHRAVKLHDNLIISDLE---------------NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI 763
Cdd:COG3883 90 ERARALYRSGGSVSYLDvllgsesfsdfldrlSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAA 169
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 764 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynymNAVERDLAALRQGMGLSRRSSTSSEPTPTVKT 843
Cdd:COG3883 170 KAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEA-------AAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAA 242
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|..
gi 1844083964 844 LIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 895
Cdd:COG3883 243 AASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGG 294
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
396-838 |
1.87e-06 |
|
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. The function is not known.
Pssm-ID: 464943 [Multi-domain] Cd Length: 1112 Bit Score: 52.43 E-value: 1.87e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSE--ELQATL-----QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRS 468
Cdd:pfam15921 80 LEEYSHQVKDLQRRLNEsnELHEKQkfylrQSVIDLQTKLQEMQMERDAMADIRRRESQSQEDLRNQLQNTVHELEAAKC 159
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 469 LldehhisyviDEDVKSGRYMELEQ-RYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMiGALKERSHHMERI 547
Cdd:pfam15921 160 L----------KEDMLEDSNTQIEQlRKMMLSHEGVLQEIRSILVDFEEASGKKIYEHDSMSTMHF-RSLGSAISKILRE 228
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 548 IESEQKGKAALAATLEEYKATVASDQieMNRLKAQLENEKQKVAELYSIHnsgdKSDIQDLLESVRLDKEKAETLASSLQ 627
Cdd:pfam15921 229 LDTEISYLKGRIFPVEDQLEALKSES--QNKIELLLQQHQDRIEQLISEH----EVEITGLTEKASSARSQANSIQSQLE 302
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 628 EDLAHTRND-------ANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQH 700
Cdd:pfam15921 303 IIQEQARNQnsmymrqLSDLESTVSQLRSELREAKRMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKL 382
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 701 RAvKLHDNLIISDLENTV-KKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTavviandIKSEAQeeiGDLKRRLH 779
Cdd:pfam15921 383 LA-DLHKREKELSLEKEQnKRLWDRDTGNSITIDHLRRELDDRNMEVQRLEALLKA-------MKSECQ---GQMERQMA 451
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083964 780 EAQEKNE------KLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQGMGLSRRS--STSSEPT 838
Cdd:pfam15921 452 AIQGKNEslekvsSLTAQLESTKEmlRKVVEELTAKKMTLESSERTVSDLTASLQEKERAieATNAEIT 520
|
|
| CH_MICALL |
cd21197 |
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family ... |
1013-1076 |
2.00e-06 |
|
calponin homology (CH) domain found in the MICAL-like protein family; The MICAL-L family includes MICAL-L1 and MICAL-L2. MICAL-L1, also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. MICAL-L2, also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this family contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409046 Cd Length: 105 Bit Score: 47.53 E-value: 2.00e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1013 KRNALLKWCQKKTEGYQR---------------------------------------RNFMLAFQAAE-SVGIKSTLDIN 1052
Cdd:cd21197 1 KIQALLRWCRRQCEGYPGvnitnltssfrdglafcailhrhrpelidfhslkkdnwlENNRLAFRVAEtSLGIPALLDAE 80
|
90 100
....*....|....*....|....
gi 1844083964 1053 EMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21197 81 DMVTMHVPDRLSIITYVSQYYNHF 104
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
619-823 |
2.09e-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: 51.30 E-value: 2.09e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 619 AETLASSLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVE 698
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKE----EKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA 93
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 699 QHRavklhdnliisdlentvKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIA---NDIKSEAQEEIGDLK 775
Cdd:COG4942 94 ELR-----------------AELEAQKEELAELLRALYRLGRQPPLALLLSPEDFLDAVRRLqylKYLAPARREQAEELR 156
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|
gi 1844083964 776 RRLHEAQEKNEKLTKELEEIKS--RKQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:COG4942 157 ADLAELAALRAELEAERAELEAllAELEEERAALEALKAERQKLLARLEK 206
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
359-791 |
2.12e-06 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 52.07 E-value: 2.12e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 359 SDDALDAPSSSESEGIPSIERSRKgssgnASEVSVACLTERIHQMEENQHSTSEEL----QATLQELADLQQITQELNSE 434
Cdd:PTZ00121 1536 ADEAKKAEEKKKADELKKAEELKK-----AEEKKKAEEAKKAEEDKNMALRKAEEAkkaeEARIEEVMKLYEEEKKMKAE 1610
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 435 NERLGEEKVILMESLcqqsDKLEHFSRQIEYFRSLLDEHHISYvidEDVKSgrymELEQRYMDLAENARFEREQllgvqQ 514
Cdd:PTZ00121 1611 EAKKAEEAKIKAEEL----KKAEEEKKKVEQLKKKEAEEKKKA---EELKK----AEEENKIKAAEEAKKAEED-----K 1674
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 515 HLSNTLKMAEQDNKEAQEMIGALKERSHHMERI--IESEQKGKAalaatlEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:PTZ00121 1675 KKAEEAKKAEEDEKKAAEALKKEAEEAKKAEELkkKEAEEKKKA------EELKKAEEENKIKAEEAKKEAEEDKKKAEE 1748
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 593 LYSihNSGDKSDIQDLLE-----SVRLDKEKAETLASSLQEDLAHTRNDANRlqdAIAKVEDEYRAFQEEAKKQIEDLNm 667
Cdd:PTZ00121 1749 AKK--DEEEKKKIAHLKKeeekkAEEIRKEKEAVIEEELDEEDEKRRMEVDK---KIKDIFDNFANIIEGGKEGNLVIN- 1822
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 668 tleklrsdlDEKETERSDMKE------TIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIktlhrrlrE 741
Cdd:PTZ00121 1823 ---------DSKEMEDSAIKEvadsknMQLEEADAFEKHKFNKNNENGEDGNKEADFNKEKDLKEDDEEEI--------E 1885
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083964 742 ESAEWRQFQADLQTAVVIANDIKSEAQEEIGD-------LKRRLHEAQEKNEKLTKE 791
Cdd:PTZ00121 1886 EADEIEKIDKDDIEREIPNNNMAGKNNDIIDDkldkdeyIKRDAEETREEIIKISKK 1942
|
|
| CH_SPTB_rpt2 |
cd21319 |
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and ... |
1012-1076 |
2.72e-06 |
|
second calponin homology (CH) domain found in spectrin beta chain, erythrocytic (SPTB) and similar proteins; Spectrin is an actin crosslinking and molecular scaffold protein that links the plasma membrane to the actin cytoskeleton, and functions in the determination of cell shape, arrangement of transmembrane proteins, and organization of organelles. It is composed of two antiparallel dimers of alpha- and beta- subunits. SPTB, also called beta-I spectrin, may be involved in anaemia pathogenesis. SPTB contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409168 Cd Length: 112 Bit Score: 47.31 E-value: 2.72e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1012 SKRNALLKWCQKKTEGY---------------------------------------QRRNFMLAFQAAE-SVGIKSTLDi 1051
Cdd:cd21319 5 SAKDALLLWCQMKTAGYpnvnvtnftsswkdglafnalihkhrpdlvdfgklkksnARHNLEHAFNVAErQLGITKLLD- 83
|
90 100
....*....|....*....|....*
gi 1844083964 1052 NEMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21319 84 PEDVFTENPDEKSIITYVVAFYHYF 108
|
|
| DUF5401 |
pfam17380 |
Family of unknown function (DUF5401); This is a family of unknown function found in ... |
378-690 |
3.26e-06 |
|
Family of unknown function (DUF5401); This is a family of unknown function found in Chromadorea.
Pssm-ID: 375164 [Multi-domain] Cd Length: 722 Bit Score: 51.28 E-value: 3.26e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 378 ERSRKGSSGNASEVsvacltERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLG-EEKVILMESLCQQSDKL 456
Cdd:pfam17380 299 ERLRQEKEEKAREV------ERRRKLEEAEKARQAEMDRQAAIYAEQERMAMERERELERIRqEERKRELERIRQEEIAM 372
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 457 EhFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRymdlaENARFEREQLLGVQQhlsntlKMAEQDNKEAQEMIGA 536
Cdd:pfam17380 373 E-ISRMRELERLQMERQQKNERVRQELEAARKVKILEE-----ERQRKIQQQKVEMEQ------IRAEQEEARQREVRRL 440
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 537 LKERSHHMERIIESEQKGKAALaatleeykATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDK 616
Cdd:pfam17380 441 EEERAREMERVRLEEQERQQQV--------ERLRQQEEERKRKKLELEKEKRDRKRAEEQRRKILEKELEERKQAMIEEE 512
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 617 EKAETLASSLQEdlahtRNDANRLQDAIAKVEDEYRAFQE-EAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:pfam17380 513 RKRKLLEKEMEE-----RQKAIYEEERRREAEEERRKQQEmEERRRIQEQMRKATEERSRLEAMEREREMMRQIV 582
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
415-792 |
3.82e-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: 51.12 E-value: 3.82e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 415 QATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDE---------DVKS 485
Cdd:TIGR00618 337 QSSIEEQRRLLQTLHSQEIHIRDAHEVATSIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCKELDilqreqatiDTRT 416
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 486 GRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHM---ERIIESEQKGKAALAATL 562
Cdd:TIGR00618 417 SAFRDLQGQLAHAKKQQELQQRYAELCAAAITCTAQCEKLEKIHLQESAQSLKEREQQLqtkEQIHLQETRKKAVVLARL 496
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 563 EEYK---------------ATVASDQIEMN-RLKAQLENEKQKVAElysihnSGDKSD--IQDLLESVRLDKEKAETLAS 624
Cdd:TIGR00618 497 LELQeepcplcgscihpnpARQDIDNPGPLtRRMQRGEQTYAQLET------SEEDVYhqLTSERKQRASLKEQMQEIQQ 570
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 625 SLQ----------EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMK------- 687
Cdd:TIGR00618 571 SFSiltqcdnrskEDIPNLQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPEQDLQDVRLHLQQCSQELALkltalha 650
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 688 -ETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQK-----------------HDMEREIKTLHRRLREESAEWRQF 749
Cdd:TIGR00618 651 lQLTLTQERVREHALSIRVLPKELLASRQLALQKMQSEKeqltywkemlaqcqtllRELETHIEEYDREFNEIENASSSL 730
|
410 420 430 440
....*....|....*....|....*....|....*....|....
gi 1844083964 750 QADLQTAVVIANDIKSEAQEEIGD-LKRRLHEAQEKNEKLTKEL 792
Cdd:TIGR00618 731 GSDLAAREDALNQSLKELMHQARTvLKARTEAHFNNNEEVTAAL 774
|
|
| HEC1 |
COG5185 |
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell ... |
504-836 |
4.01e-06 |
|
Chromosome segregation protein NDC80, interacts with SMC proteins [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 444066 [Multi-domain] Cd Length: 594 Bit Score: 50.73 E-value: 4.01e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 504 FEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKE--RSHHMERIIESEQKGKAaLAATLEEYKATV-ASDQIEMNRLK 580
Cdd:COG5185 193 SELKKAEPSGTVNSIKESETGNLGSESTLLEKAKEIinIEEALKGFQDPESELED-LAQTSDKLEKLVeQNTDLRLEKLG 271
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 581 AQLENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQ-EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAK 659
Cdd:COG5185 272 ENAESSKRLNEN-----ANNLIKQFENTKEKIAEYTKSIDIKKATESlEEQLAAAEAEQELEESKRETETGIQNLTAEIE 346
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 660 KQIEDLNMTLEKLRSDLDEKETER--SDMKETIFELEDEVE--------QHRAVKLHDNLIISDLENTVKKLQDQKHDME 729
Cdd:COG5185 347 QGQESLTENLEAIKEEIENIVGEVelSKSSEELDSFKDTIEstkesldeIPQNQRGYAQEILATLEDTLKAADRQIEELQ 426
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 730 REIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRlhEAQEKNEKLTKELEEIKSRKQeEERGRVYN 809
Cdd:COG5185 427 RQIEQATSSNEEVSKLLNELISELNKVMREADEESQSRLEEAYDEINR--SVRSKKEDLNEELTQIESRVS-TLKATLEK 503
|
330 340
....*....|....*....|....*..
gi 1844083964 810 YMNAVERDLAALRQGMGLSRRSSTSSE 836
Cdd:COG5185 504 LRAKLERQLEGVRSKLDQVAESLKDFM 530
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
570-798 |
4.53e-06 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 51.07 E-value: 4.53e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 570 ASDQIEmnRLKAQLENEKQKVAELYSihnsgDKSDIQDLLESVRLDKEKAETLASSLQEDLahtrnDANRLQDAIAKVED 649
Cdd:COG4913 608 NRAKLA--ALEAELAELEEELAEAEE-----RLEALEAELDALQERREALQRLAEYSWDEI-----DVASAEREIAELEA 675
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 650 EYRAFQ------EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAV-----------------KLH 706
Cdd:COG4913 676 ELERLDassddlAALEEQLEELEAELEELEEELDELKGEIGRLEKELEQAEEELDELQDRleaaedlarlelralleERF 755
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 707 DNLIISDLENTVKK-LQDQKHDMEREIKTLHRRLREE----SAEWRQFQADLQTAV-----------VIANDIKSEAQEE 770
Cdd:COG4913 756 AAALGDAVERELREnLEERIDALRARLNRAEEELERAmrafNREWPAETADLDADLeslpeylalldRLEEDGLPEYEER 835
|
250 260 270
....*....|....*....|....*....|...
gi 1844083964 771 igdLKRRLHEAQEK-----NEKLTKELEEIKSR 798
Cdd:COG4913 836 ---FKELLNENSIEfvadlLSKLRRAIREIKER 865
|
|
| CH_SpAIN1-like_rpt2 |
cd21291 |
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like ... |
1008-1076 |
4.97e-06 |
|
second calponin homology (CH) domain found in Schizosaccharomyces pombe alpha-actinin-like protein 1 and similar proteins; Schizosaccharomyces pombe alpha-actinin-like protein 1 (SpAIN1) binds to actin and is involved in actin-ring formation and organization. It plays a role in cytokinesis and is involved in septation. Members of this family contain two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409140 Cd Length: 115 Bit Score: 46.75 E-value: 4.97e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1008 EYGGSKRNALLKWCQKKTEGY---------------------------------------QRRNFMLAFQ-AAESVGIKS 1047
Cdd:cd21291 6 EEGLTAKEGLLLWCQRKTAGYdevdvqdfttswtdglafcalihrhrpdlidydkldkkdHRGNMQLAFDiASKEIGIPQ 85
|
90 100
....*....|....*....|....*....
gi 1844083964 1048 TLDINEMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21291 86 LLDVEDVCDVAKPDERSIMTYVAYYFHAF 114
|
|
| CH_SMTNB |
cd21259 |
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are ... |
1012-1074 |
5.63e-06 |
|
calponin homology (CH) domain found in smoothelin-B and similar proteins; Smoothelins are actin-binding cytoskeletal proteins that are abundantly expressed in healthy visceral (smoothelin-A) and vascular (smoothelin-B) smooth muscle. The human SMTN gene encodes smoothelin-A and smoothelin-B. This model corresponds to the single CH domain of smoothelin-B. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409108 Cd Length: 112 Bit Score: 46.52 E-value: 5.63e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1012 SKRNALLKWCQKKTEGYQ---------------------------------------RRNFMLAFQAAES-VGIKSTLDI 1051
Cdd:cd21259 1 SIKQMLLDWCRAKTRGYEnvdiqnfssswsdgmafcalvhnffpeafdysqlspqnrRHNFEVAFSSAEKhADCPQLLDV 80
|
90 100
....*....|....*....|...
gi 1844083964 1052 NEMVRTERPDWQNVMLYVTAIYK 1074
Cdd:cd21259 81 EDMVRMREPDWKCVYTYIQEFYR 103
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
601-804 |
7.41e-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: 49.38 E-value: 7.41e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 601 DKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAK---KQIEDLNMTLEKLRSDLD 677
Cdd:COG4942 21 AAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAaleAELAELEKEIAELRAELE 100
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 678 EKETERSDMKETIFELEdeveQHRAVKLHdnLIISDLENTVKKLQDQKHdMEREIKTLHRRLREESAEWRQFQADLQTAV 757
Cdd:COG4942 101 AQKEELAELLRALYRLG----RQPPLALL--LSPEDFLDAVRRLQYLKY-LAPARREQAEELRADLAELAALRAELEAER 173
|
170 180 190 200
....*....|....*....|....*....|....*....|....*..
gi 1844083964 758 VIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG4942 174 AELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQ 220
|
|
| CH_MICALL2 |
cd21253 |
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like ... |
1016-1077 |
7.51e-06 |
|
calponin homology (CH) domain found in MICAL-like protein 2 and similar proteins; MICAL-like protein 2 (MICAL-L2), also called junctional Rab13-binding protein (JRAB), or molecule interacting with CasL-like 2, acts as an effector of small Rab GTPases which is involved in junctional complexes assembly through the regulation of cell adhesion molecule transport to the plasma membrane, and actin cytoskeleton reorganization. It regulates the endocytic recycling of occludins, claudins, and E-cadherin to the plasma membrane and may thereby regulate the establishment of tight junctions and adherens junctions. Members of this subfamily contain a single copy of CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409102 Cd Length: 106 Bit Score: 45.80 E-value: 7.51e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1016 ALLKWCQKKTEGYQ---------------------------------------RRNFMLAFQAAES-VGIKSTLDINEMV 1055
Cdd:cd21253 5 ALQQWCRQQTEGYRdvkvtnmttswrdglafcaiihrfrpdlidfdslskenvYENNKLAFTVAEKeLGIPALLDAEDMV 84
|
90 100
....*....|....*....|..
gi 1844083964 1056 RTERPDWQNVMLYVTAIYKYFE 1077
Cdd:cd21253 85 ALKVPDKLSILTYVSQYYNYFH 106
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
378-822 |
1.30e-05 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 49.68 E-value: 1.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 378 ERSRKGSSGNASEVSVACLTERIHQM-EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKL 456
Cdd:TIGR02169 259 EISELEKRLEEIEQLLEELNKKIKDLgEEEQLRVKEKIGELEAEIASLERSIAEKERELEDAEERLAKLEAEIDKLLAEI 338
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 457 EHFSRQIEYFRSLLDEHHISYVIDEDVksgrYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGA 536
Cdd:TIGR02169 339 EELEREIEEERKRRDKLTEEYAELKEE----LEDLRAELEEVDKEFAETRDELKDYREKLEKLKREINELKRELDRLQEE 414
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 537 LKERSHHMERI---IESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQkvaELYSIHNsgDKSDIQDLLESVR 613
Cdd:TIGR02169 415 LQRLSEELADLnaaIAGIEAKINELEEEKEDKALEIKKQEWKLEQLAADLSKYEQ---ELYDLKE--EYDRVEKELSKLQ 489
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAI----------AKVEDEYRAFQE----------------EAKKQIEDLN- 666
Cdd:TIGR02169 490 RELAEAEAQARASEERVRGGRAVEEVLKASIqgvhgtvaqlGSVGERYATAIEvaagnrlnnvvveddaVAKEAIELLKr 569
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 667 -----MT---LEKLRSDldEKETERSDMKETI------FELEDEVEQHRAVKLHDNLIISDLENT--------------- 717
Cdd:TIGR02169 570 rkagrATflpLNKMRDE--RRDLSILSEDGVIgfavdlVEFDPKYEPAFKYVFGDTLVVEDIEAArrlmgkyrmvtlege 647
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 718 ----------------------------VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLqtavviandikSEAQE 769
Cdd:TIGR02169 648 lfeksgamtggsraprggilfsrsepaeLQRLRERLEGLKRELSSLQSELRRIENRLDELSQEL-----------SDASR 716
|
490 500 510 520 530
....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 770 EIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALR 822
Cdd:TIGR02169 717 KIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEI-----ENVKSELKELE 764
|
|
| CH_EHBP |
cd21198 |
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP ... |
1017-1076 |
1.65e-05 |
|
calponin homology (CH) domain found in the EH domain-binding protein (EHBP) family; The EHBP family includes EHBP1 and EHBP1-like protein (EHBP1L1). EHBP1 is a regulator of endocytic recycling and may play a role in actin reorganization by linking clathrin-mediated endocytosis to the actin cytoskeleton. It may act as an effector of small GTPases, including RAB-10 (Rab10), and play a role in vesicle trafficking. EHBP1 is associated with aggressive prostate cancer and insulin-stimulated trafficking and cell migration. EHBP1L1 may also act as Rab effector protein and play a role in vesicle trafficking. It coordinates Rab8 and Bin1 to regulate apical-directed transport in polarized epithelial cells. Members of this family contain a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409047 Cd Length: 105 Bit Score: 44.72 E-value: 1.65e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1017 LLKWCQKKTEGYQ---------------------------------------RRNFMLAFQAAESVGIKSTLDINEMVRT 1057
Cdd:cd21198 6 LLEWCQEVTKGYRgvkitnlttswrnglafcailhhfrpdlidfsslsphdiKENCKLAFDAAAKLGIPRLLDPADMVLL 85
|
90
....*....|....*....
gi 1844083964 1058 ERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21198 86 SVPDKLSVMTYLHQIRAHF 104
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
398-822 |
1.80e-05 |
|
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: 49.07 E-value: 1.80e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 398 ERIHQMEENQHS--------TSEELQA-TLQELAD--LQQITQELNSENERLGEekviLMESLCQQSDKLEHFSRQieyf 466
Cdd:pfam12128 471 ERIERAREEQEAanaeverlQSELRQArKRRDQASeaLRQASRRLEERQSALDE----LELQLFPQAGTLLHFLRK---- 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 467 RSLLDEHHISYVIDEdvksgrymELEQRyMDLaeNARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMER 546
Cdd:pfam12128 543 EAPDWEQSIGKVISP--------ELLHR-TDL--DPEVWDGSVGGELNLYGVKLDLKRIDVPEWAASEEELRERLDKAEE 611
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 547 IIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSgdksdiqdllESVRLDKEKAETLASSL 626
Cdd:pfam12128 612 ALQSAREKQAAAEEQLVQANGELEKASREETFARTALKNARLDLRRLFDEKQS----------EKDKKNKALAERKDSAN 681
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 627 QE--DLAHTRNdanrlqdaiaKVEDEYRAFQEEAKKQIEDLNMT-LEKLRSDLDEKETERSDMKETIFELEdevEQHRAv 703
Cdd:pfam12128 682 ERlnSLEAQLK----------QLDKKHQAWLEEQKEQKREARTEkQAYWQVVEGALDAQLALLKAAIAARR---SGAKA- 747
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 704 klHDNLIISDLENTVKKL---QDQKHDMEREIKTLHRRL------REESAEWRQFQADL-----QTAVVIANDIKSEAQE 769
Cdd:pfam12128 748 --ELKALETWYKRDLASLgvdPDVIAKLKREIRTLERKIeriavrRQEVLRYFDWYQETwlqrrPRLATQLSNIERAISE 825
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 770 EIGDLKRRLHEAQEKNEKLTKELEeiKSRKQEEERGRVYNYMNAVERDLAALR 822
Cdd:pfam12128 826 LQQQLARLIADTKLRRAKLEMERK--ASEKQQVRLSENLRGLRCEMSKLATLK 876
|
|
| PRK02224 |
PRK02224 |
DNA double-strand break repair Rad50 ATPase; |
412-681 |
1.97e-05 |
|
DNA double-strand break repair Rad50 ATPase;
Pssm-ID: 179385 [Multi-domain] Cd Length: 880 Bit Score: 48.88 E-value: 1.97e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 412 EELQAtlqELADLQQITQELNSENERLgeekvilmESLCQQSDKLEHFSRQIEYFRSLLDEHHISyvIDEDvkSGRYMEL 491
Cdd:PRK02224 478 EELEA---ELEDLEEEVEEVEERLERA--------EDLVEAEDRIERLEERREDLEELIAERRET--IEEK--RERAEEL 542
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 492 EQRYMDLAENARFEREQLlgvqqhlsntlKMAEQDNKEAQEMIGALKERSHHMERIIESEQKgKAALAATLEEYKATVAS 571
Cdd:PRK02224 543 RERAAELEAEAEEKREAA-----------AEAEEEAEEAREEVAELNSKLAELKERIESLER-IRTLLAAIADAEDEIER 610
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 572 ------DQIEMNRL-KAQLENEKQKVAELYSIHNsgdksdiQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAI 644
Cdd:PRK02224 611 lrekreALAELNDErRERLAEKRERKRELEAEFD-------EARIEEAREDKERAEEYLEQVEEKLDELREERDDLQAEI 683
|
250 260 270
....*....|....*....|....*....|....*..
gi 1844083964 645 AKVEDEYRAFqEEAKKQIEDLNMTLEKLRSDLDEKET 681
Cdd:PRK02224 684 GAVENELEEL-EELRERREALENRVEALEALYDEAEE 719
|
|
| DR0291 |
COG1579 |
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General ... |
538-678 |
2.06e-05 |
|
Predicted nucleic acid-binding protein DR0291, contains C4-type Zn-ribbon domain [General function prediction only];
Pssm-ID: 441187 [Multi-domain] Cd Length: 236 Bit Score: 47.23 E-value: 2.06e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 538 KERSHHMERIIESEQKgKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE----LYSIHNSGDKSDIQDLLESVR 613
Cdd:COG1579 24 HRLKELPAELAELEDE-LAALEARLEAAKTELEDLEKEIKRLELEIEEVEARIKKyeeqLGNVRNNKEYEALQKEIESLK 102
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDE 678
Cdd:COG1579 103 RRISDLEDEILELMERIEELEEELAELEAELAELEAELEEKKAELDEELAELEAELEELEAEREE 167
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-801 |
2.20e-05 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 48.78 E-value: 2.20e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHI 475
Cdd:COG1196 307 LEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAE 386
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 476 SY------VIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIE 549
Cdd:COG1196 387 ELlealraAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEALLELLA 466
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 550 SEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAET-----LAS 624
Cdd:COG1196 467 ELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLAGAVAVLIGVEAAYEAaleaaLAA 546
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 625 SLQEDLAHTRNDA------------------------------------------NRLQDAIAKVEDEYRAFQE------ 656
Cdd:COG1196 547 ALQNIVVEDDEVAaaaieylkaakagratflpldkiraraalaaalargaigaavDLVASDLREADARYYVLGDtllgrt 626
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 657 ---------------------EAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLE 715
Cdd:COG1196 627 lvaarleaalrravtlagrlrEVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLAEEEEE 706
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 716 NTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTK----- 790
Cdd:COG1196 707 RELAEAEEERLEEELEEEALEEQLEAEREELLEELLEEEELLEEEALEELPEPPDLEELERELERLEREIEALGPvnlla 786
|
490
....*....|...
gi 1844083964 791 --ELEEIKSRKQE 801
Cdd:COG1196 787 ieEYEELEERYDF 799
|
|
| COG5022 |
COG5022 |
Myosin heavy chain [General function prediction only]; |
491-968 |
3.61e-05 |
|
Myosin heavy chain [General function prediction only];
Pssm-ID: 227355 [Multi-domain] Cd Length: 1463 Bit Score: 48.15 E-value: 3.61e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 491 LEQRYMDLAENARFEReQLLGVQQHLSNTLKmAEQDNKEAQEMIGALKERSHHmERIIESEQKGKAALaatLEEYKATVA 570
Cdd:COG5022 798 KLQPLLSLLGSRKEYR-SYLACIIKLQKTIK-REKKLRETEEVEFSLKAEVLI-QKFGRSLKAKKRFS---LLKKETIYL 871
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 571 SDQIEMNRLKAQLENEKQKVAELYSIHNSGDKsdiqdlLESVRLdkEKAETLASSLQEDLAHTRNDANRLQDAIAKVE-D 649
Cdd:COG5022 872 QSAQRVELAERQLQELKIDVKSISSLKLVNLE------LESEII--ELKKSLSSDLIENLEFKTELIARLKKLLNNIDlE 943
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 650 EYRAFQEEAKKQIEDLNMtleklrsdldeketERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQ---DQKH 726
Cdd:COG5022 944 EGPSIEYVKLPELNKLHE--------------VESKLKETSEEYEDLLKKSTILVREGNKANSELKNFKKELAelsKQYG 1009
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 727 DMEREIKTLHRRLREesaewrqfQADLQTAVVIANDIKSEAQ--EEIGDLKRRL------HEAQEKNEKLTKELEEIKSr 798
Cdd:COG5022 1010 ALQESTKQLKELPVE--------VAELQSASKIISSESTELSilKPLQKLKGLLllennqLQARYKALKLRRENSLLDD- 1080
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 799 KQEEERGRVYNYMNAVERD--LAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQVPNpaaaaiprtPLSPSPMKTPP 876
Cdd:COG5022 1081 KQLYQLESTENLLKTINVKdlEVTNRNLVKPANVLQFIVAQMIKLNLLQEISKFLSQLVN---------TLEPVFQKLSV 1151
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 877 A-AAVSPMQRHSISGPISTSKPLTALSDKRpnygeiPVQEHLLRTSSASRPASLPrvpaMESAKTLSVSRRSSEEVKRDI 955
Cdd:COG5022 1152 LqLELDGLFWEANLEALPSPPPFAALSEKR------LYQSALYDEKSKLSSSEVN----DLKNELIALFSKIFSGWPRGD 1221
|
490
....*....|...
gi 1844083964 956 SAQEGASPASLMA 968
Cdd:COG5022 1222 KLKKLISEGWVPT 1234
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-804 |
3.69e-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: 47.71 E-value: 3.69e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKAQLENEKQKVAElysihnsgDKSDIQDLLESVRLDKEKAETLASSLQE----------DLAHTRNDANRLQDAI 644
Cdd:TIGR04523 163 DLKKQKEELENELNLLEK--------EKLNIQKNIDKIKNKLLKLELLLSNLKKkiqknkslesQISELKKQNNQLKDNI 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 645 AKVEDEYRAFQEE---AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENtvKKL 721
Cdd:TIGR04523 235 EKKQQEINEKTTEisnTQTQLNQLKDEQNKIKKQLSEKQKELEQNNKKIKELEKQLNQLKSE-------ISDLNN--QKE 305
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 722 QDQKHDMEREIKTLHRRLREesaewrqfqadLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR04523 306 QDWNKELKSELKNQEKKLEE-----------IQNQISQNNKIISQLNEQISQLKKELTNSESENSEKQRELEEKQNEIEK 374
|
...
gi 1844083964 802 EER 804
Cdd:TIGR04523 375 LKK 377
|
|
| ClyA_Cry6Aa-like |
cd22656 |
Bacillus thuringiensis crystal 6Aa (Cry6Aa) toxin, and similar proteins; This model includes ... |
604-737 |
4.63e-05 |
|
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: 46.59 E-value: 4.63e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 604 DIQDLLESVrlDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ---EEAKKQIEDLNMTLEKLRSDlDEKE 680
Cdd:cd22656 99 LIDDLADAT--DDEELEEAKKTIKALLDDLLKEAKKYQDKAAKVVDKLTDFEnqtEKDQTALETLEKALKDLLTD-EGGA 175
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083964 681 TERSDMKetifELEDEVEQHRAVklhdnlIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:cd22656 176 IARKEIK----DLQKELEKLNEE------YAAKLKAKIDELKALIADDEAKLAAALR 222
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
604-807 |
6.87e-05 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 47.26 E-value: 6.87e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 604 DIQDLLESVRLDKEKAETLASSLQedlahtrndanRLQDAIAKVEDEYRAFQEEAKKqiedlnmtLEKLRSDLDEKETER 683
Cdd:PRK04863 891 TLADRVEEIREQLDEAEEAKRFVQ-----------QHGNALAQLEPIVSVLQSDPEQ--------FEQLKQDYQQAQQTQ 951
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 684 SDMKETIFELEDEVEQHRAVKLHDNLII----SDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVI 759
Cdd:PRK04863 952 RDAKQQAFALTEVVQRRAHFSYEDAAEMlaknSDLNEKLRQRLEQAEQERTRAREQLRQAQAQLAQYNQVLASLKSSYDA 1031
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 760 ANDIKSEAQEEIGDLKRRLHE-----AQEKNEKLTKELEEIKSRKQEEERGRV 807
Cdd:PRK04863 1032 KRQMLQELKQELQDLGVPADSgaeerARARRDELHARLSANRSRRNQLEKQLT 1084
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
575-819 |
7.68e-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: 46.94 E-value: 7.68e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKAQLENEKQKVAELYS--------IHNSGDKSDIQDLLESVRLDKEKAE-TLASSLQEDLAHTRNDANRLQDAIA 645
Cdd:TIGR04523 41 KLKTIKNELKNKEKELKNLDKnlnkdeekINNSNNKIKILEQQIKDLNDKLKKNkDKINKLNSDLSKINSEIKNDKEQKN 120
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 646 KVEDEYRAFQEEAK---KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDE--------------VEQHRAVKLHDN 708
Cdd:TIGR04523 121 KLEVELNKLEKQKKenkKNIDKFLTEIKKKEKELEKLNNKYNDLKKQKEELENElnllekeklniqknIDKIKNKLLKLE 200
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 709 LIISDLENTVKK---LQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKN 785
Cdd:TIGR04523 201 LLLSNLKKKIQKnksLESQISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQKELEQNN 280
|
250 260 270
....*....|....*....|....*....|....*..
gi 1844083964 786 EK---LTKELEEIKSRKQEEERGRVYNYMNAVERDLA 819
Cdd:TIGR04523 281 KKikeLEKQLNQLKSEISDLNNQKEQDWNKELKSELK 317
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
464-702 |
1.14e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 46.45 E-value: 1.14e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 464 EYFRSL-LDEHHISYVIDEDVKS-GRYMELEQRymdlAENARFEREQLLGVQQHLSntlkmAEQDNKEAQEMIGALKERS 541
Cdd:COG4913 211 DFVREYmLEEPDTFEAADALVEHfDDLERAHEA----LEDAREQIELLEPIRELAE-----RYAAARERLAELEYLRAAL 281
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 542 HHMERiieseQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNS---GDKSDIQDLLESVRLDKEK 618
Cdd:COG4913 282 RLWFA-----QRRLELLEAELEELRAELARLEAELERLEARLDALREELDELEAQIRGnggDRLEQLEREIERLERELEE 356
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 619 AETLASSLQ--------------EDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmtlekLRSDLDEKETERS 684
Cdd:COG4913 357 RERRRARLEallaalglplpasaEEFAALRAEAAALLEALEEELEALEEALAEAEAALRD-------LRRELRELEAEIA 429
|
250
....*....|....*...
gi 1844083964 685 DMKETIFELEDEVEQHRA 702
Cdd:COG4913 430 SLERRKSNIPARLLALRD 447
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
396-678 |
1.19e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 46.47 E-value: 1.19e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG1196 244 LEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERLEE--- 320
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 476 sYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERshhmERIIESEQKGK 555
Cdd:COG1196 321 -LEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEEL----AEELLEALRAA 395
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 556 AALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRN 635
Cdd:COG1196 396 AELAAQLEELEEAEEALLERLERLEEELEELEEALAEL-----EEEEEEEEEALEEAAEEEAELEEEEEALLELLAELLE 470
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844083964 636 DANRLQDAIAKVEDEyrafqEEAKKQIEDLNMTLEKLRSDLDE 678
Cdd:COG1196 471 EAALLEAALAELLEE-----LAEAAARLLLLLEAEADYEGFLE 508
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
602-816 |
1.27e-04 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 46.21 E-value: 1.27e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 602 KSDIQDLLesvrldKEKAETLASSLQEdLAHTRNDANRLQDAIAKVEDEYRAFQE------EAKKQIEDLNMTLEKLRSD 675
Cdd:PRK03918 188 TENIEELI------KEKEKELEEVLRE-INEISSELPELREELEKLEKEVKELEElkeeieELEKELESLEGSKRKLEEK 260
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 676 LDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIIsdlenTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQT 755
Cdd:PRK03918 261 IRELEERIEELKKEIEELEEKVKELKELKEKAEEYI-----KLSEFYEEYLDELREIEKRLSRLEEEINGIEERIKELEE 335
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 1844083964 756 AVVIANDIK---SEAQEEIGDLKRRlHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVER 816
Cdd:PRK03918 336 KEERLEELKkklKELEKRLEELEER-HELYEEAKAKKEELERLKKRLTGLTPEKLEKELEELEK 398
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
363-822 |
1.40e-04 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 46.05 E-value: 1.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 363 LDAPSSSESEGIPSIER--------SRKGSSGNASEVSVACLTERIHQMEENQHSTSEELQATLQELADLQQITQELNS- 433
Cdd:PRK01156 206 IADDEKSHSITLKEIERlsieynnaMDDYNNLKSALNELSSLEDMKNRYESEIKTAESDLSMELEKNNYYKELEERHMKi 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 434 ENERLGEEKVILMESLCQQSDkLEHFSRQIEYFRSLLDEHHISYVIDEDVKSGR--YMELEQRYMDLAEnarfEREQLLG 511
Cdd:PRK01156 286 INDPVYKNRNYINDYFKYKND-IENKKQILSNIDAEINKYHAIIKKLSVLQKDYndYIKKKSRYDDLNN----QILELEG 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 512 VQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVA 591
Cdd:PRK01156 361 YEMDYNSYLKSIESLKKKIEEYSKNIERMSAFISEILKIQEIDPDAIKKELNEINVKLQDISSKVSSLNQRIRALRENLD 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 592 ELysihnsgdkSDIQDLLESVRLDKEKAETLASSLQEDLA-HTRNDANRLQDAIAKVEDEYRAFQEEAKKQI-------- 662
Cdd:PRK01156 441 EL---------SRNMEMLNGQSVCPVCGTTLGEEKSNHIInHYNEKKSRLEEKIREIEIEVKDIDEKIVDLKkrkeyles 511
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 663 EDLNMT------LEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHD-----------NLIISDLEntVKKLQDQK 725
Cdd:PRK01156 512 EEINKSineynkIESARADLEDIKIKINELKDKHDKYEEIKNRYKSLKLEDldskrtswlnaLAVISLID--IETNRSRS 589
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 726 HDMEREIKTLHRRLREESAEWRQFQADLQTAV-VIANDIKS--EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRkqEE 802
Cdd:PRK01156 590 NEIKKQLNDLESRLQEIEIGFPDDKSYIDKSIrEIENEANNlnNKYNEIQENKILIEKLRGKIDNYKKQIAEIDSI--IP 667
|
490 500
....*....|....*....|
gi 1844083964 803 ERGRVYNYMNAVERDLAALR 822
Cdd:PRK01156 668 DLKEITSRINDIEDNLKKSR 687
|
|
| CH_MICALL1 |
cd21252 |
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), ... |
1032-1076 |
1.47e-04 |
|
calponin homology (CH) domain found in MICAL-like protein 1; MICAL-like protein 1 (MICAL-L1), also called molecule interacting with Rab13 (MIRab13), is a probable lipid-binding protein with higher affinity for phosphatidic acid, a lipid enriched in recycling endosome membranes. It is a tubular endosomal membrane hub that connects Rab35 and Arf6 with Rab8a. It may be involved in a late step of receptor-mediated endocytosis regulating endocytosed-EGF receptor trafficking. Alternatively, it may regulate slow endocytic recycling of endocytosed proteins back to the plasma membrane. MICAL-L1 may indirectly play a role in neurite outgrowth. It contains a single copy of the CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409101 Cd Length: 107 Bit Score: 42.16 E-value: 1.47e-04
10 20 30 40
....*....|....*....|....*....|....*....|....*.
gi 1844083964 1032 NFMLAFQAAES-VGIKSTLDINEMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21252 59 NNRLAFEVAEReLGIPALLDPEDMVSMKVPDCLSIMTYVSQYYNHF 104
|
|
| Rabaptin |
pfam03528 |
Rabaptin; |
614-823 |
1.67e-04 |
|
Rabaptin;
Pssm-ID: 367545 [Multi-domain] Cd Length: 486 Bit Score: 45.48 E-value: 1.67e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYR--AFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIF 691
Cdd:pfam03528 13 LEKENAEFYRLKQQLEAEFNQKRAKFKELYLAKEEDLKRqnAVLQEAQVELDALQNQLALARAEMENIKAVATVSENTKQ 92
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 692 ELEDEVEqhravklhdnliiSDLENTVKKLQDQKHDMEREIK-TLHRRLREESAEWRQFqadlqtavviandiKSEAQEE 770
Cdd:pfam03528 93 EAIDEVK-------------SQWQEEVASLQAIMKETVREYEvQFHRRLEQERAQWNQY--------------RESAERE 145
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 771 IGDLKRRLHEAQEKnEKLTKELeeiksRKQEEERGRVYNYMNAVERDLAALRQ 823
Cdd:pfam03528 146 IADLRRRLSEGQEE-ENLEDEM-----KKAQEDAEKLRSVVMPMEKEIAALKA 192
|
|
| CALCOCO1 |
pfam07888 |
Calcium binding and coiled-coil domain (CALCOCO1) like; Proteins found in this family are ... |
618-833 |
1.69e-04 |
|
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: 45.66 E-value: 1.69e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 618 KAETLASSLQEDLaHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDlnmTLEKLRSDLDEKETERSDMKETIFELE--- 694
Cdd:pfam07888 28 RAELLQNRLEECL-QERAELLQAQEAANRQREKEKERYKRDREQWER---QRRELESRVAELKEELRQSREKHEELEeky 103
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 695 -------DEVEQHRAVKLHDN----LIISDLENTVKKLQDQKHDMEREI-------KTLHRRLREESAEWRQFQADLQTA 756
Cdd:pfam07888 104 kelsassEELSEEKDALLAQRaaheARIRELEEDIKTLTQRVLERETELermkeraKKAGAQRKEEEAERKQLQAKLQQT 183
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083964 757 VVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvynyMNAVERDLAALRQGMGLSRRSST 833
Cdd:pfam07888 184 EEELRSLSKEFQELRNSLAQRDTQVLQLQDTITTLTQKLTTAHRKEAE------NEALLEELRSLQERLNASERKVE 254
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
398-804 |
1.71e-04 |
|
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: 45.81 E-value: 1.71e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 398 ERIHQMEENQHSTSEELQatlQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHISY 477
Cdd:TIGR00606 301 EQLNDLYHNHQRTVREKE---RELVDCQRELEKLNKERRLLNQEKTELLVEQGRLQLQADRHQEHIRARDSLIQSLATRL 377
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 478 VIDE-------DVKSGRYMELEQRYM------------DLAENARFEREQL-------LGVQQHLSNTLKMAEQDNKEAQ 531
Cdd:TIGR00606 378 ELDGfergpfsERQIKNFHTLVIERQedeaktaaqlcaDLQSKERLKQEQAdeirdekKGLGRTIELKKEILEKKQEELK 457
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 532 EMIGALKERSHHMERIIESEQKGKAALA--------ATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS 603
Cdd:TIGR00606 458 FVIKELQQLEGSSDRILELDQELRKAERelskaeknSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQM 537
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 604 -----DIQDLLESVRLDKEKAETLASSLQEDLAHT----------RNDANRLQDAIAKVEDEYrAFQEEAKKQIEDLNMT 668
Cdd:TIGR00606 538 emltkDKMDKDEQIRKIKSRHSDELTSLLGYFPNKkqledwlhskSKEINQTRDRLAKLNKEL-ASLEQNKNHINNELES 616
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 669 LEKLRSDLDEK-------ETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTlhrrlre 741
Cdd:TIGR00606 617 KEEQLSSYEDKlfdvcgsQDEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDENQSCCPVCQRVFQT------- 689
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 742 eSAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRR---------------------LHEAQEKNEKLTKELEEIKSRKQ 800
Cdd:TIGR00606 690 -EAELQEFISDLQSKLRLAPDKLKSTESELKKKEKRrdemlglapgrqsiidlkekeIPELRNKLQKVNRDIQRLKNDIE 768
|
....
gi 1844083964 801 EEER 804
Cdd:TIGR00606 769 EQET 772
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
827-992 |
1.91e-04 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 45.70 E-value: 1.91e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 827 LSRRSSTSSEPT---------------PTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGP 891
Cdd:PHA03247 2663 RPRRARRLGRAAqassppqrprrraarPTVGSLTSLADPPPPPPTPEPAPHALVSATPLPPGPAAARQASPALPAAPAPP 2742
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 892 ISTSKPLTALSDKRPNYGEIPvqehllrtSSASRPASlPRVPAMESAKTLSVSRRSSEEVKRDiSAQEGASPASLMAMGT 971
Cdd:PHA03247 2743 AVPAGPATPGGPARPARPPTT--------AGPPAPAP-PAAPAAGPPRRLTRPAVASLSESRE-SLPSPWDPADPPAAVL 2812
|
170 180
....*....|....*....|.
gi 1844083964 972 TSPQLSLSSSPTASVTPTTRS 992
Cdd:PHA03247 2813 APAAALPPAASPAGPLPPPTS 2833
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
172-802 |
1.96e-04 |
|
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: 45.49 E-value: 1.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 172 DNQISDRAALEAKVKDLLTLAKTKDVEILHLRNELRDMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQ-- 249
Cdd:pfam15921 230 DTEISYLKGRIFPVEDQLEALKSESQNKIELLLQQHQDRIEQLISEHEVEITGLTEKASSARSQANSIQSQLEIIQEQar 309
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 250 --NTAIREELNQLKNENRMLKDRLNALGFSLEQRLDNSEK--LFGYQSLSPEITPGNQ-SDGGGTLTSSVEGSAPG---- 320
Cdd:pfam15921 310 nqNSMYMRQLSDLESTVSQLRSELREAKRMYEDKIEELEKqlVLANSELTEARTERDQfSQESGNLDDQLQKLLADlhkr 389
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 321 SVEDLLSQDENT-LMDHQHSNSM--DNLDSECSEVYQPLTSSDDALDApSSSESEGipSIERSRKGSSG-NASEVSVACL 396
Cdd:pfam15921 390 EKELSLEKEQNKrLWDRDTGNSItiDHLRRELDDRNMEVQRLEALLKA-MKSECQG--QMERQMAAIQGkNESLEKVSSL 466
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 397 TERIHQMEENQHSTSEELQATLQELADLQQITQELNSenerlgeekvilmeSLCQQSDKLEHFSRQIEYFRSLldehhis 476
Cdd:pfam15921 467 TAQLESTKEMLRKVVEELTAKKMTLESSERTVSDLTA--------------SLQEKERAIEATNAEITKLRSR------- 525
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 477 yvIDEDVKSGRYMELEQRYMdlaENARFEREQLlgvqqhlsnTLKMAEQDnkeaqEMIGALKERSHHMERIIESEQKGKA 556
Cdd:pfam15921 526 --VDLKLQELQHLKNEGDHL---RNVQTECEAL---------KLQMAEKD-----KVIEILRQQIENMTQLVGQHGRTAG 586
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 557 ALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDL-LESVRLDKEKAETLAS---------SL 626
Cdd:pfam15921 587 AMQVEKAQLEKEINDRRLELQEFKILKDKKDAKIREL--------EARVSDLeLEKVKLVNAGSERLRAvkdikqerdQL 658
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 627 QEDLAHTRNDANRLQdaiakveDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLH 706
Cdd:pfam15921 659 LNEVKTSRNELNSLS-------EDYEVLKRNFRNKSEEMETTTNKLKMQLKSAQSELEQTRNTLKSMEGSDGHAMKVAMG 731
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 707 DNLIISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAqEEIGDLKRRLHE------ 780
Cdd:pfam15921 732 MQKQITAKRGQIDALQSKIQFLEEAMTNANKEKHFLKEEKNKLSQELSTVATEKNKMAGEL-EVLRSQERRLKEkvanme 810
|
650 660
....*....|....*....|...
gi 1844083964 781 -AQEKNEKLTKELEEIKSRKQEE 802
Cdd:pfam15921 811 vALDKASLQFAECQDIIQRQEQE 833
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
606-895 |
2.40e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 44.82 E-value: 2.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 606 QDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDE---- 678
Cdd:COG3883 15 DPQIQAKQKELSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKlqaEIAEAEAEIEERREELGErara 94
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 679 --KETERSDMKETIF------ELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLhrrlreesaewRQFQ 750
Cdd:COG3883 95 lyRSGGSVSYLDVLLgsesfsDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAEL-----------EALK 163
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 751 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRvynymNAVERDLAALRQGMGLSRR 830
Cdd:COG3883 164 AELEAAKAELEAQQAEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAA-----AAAAAAAAAAAAAAAAAAA 238
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 831 SSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAVSPMQRHSISGPISTS 895
Cdd:COG3883 239 AAAAAASAAGAGAAGAAGAAAGSAGAAGAAAGAAGAGAAAASAAGGGAGGAGGGGGGGGAASGGS 303
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
635-802 |
2.79e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 45.20 E-value: 2.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 635 NDANRLQDAIAKVEDEYRAfQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIF-ELEDEVEQH-RAVKLHDNLIIS 712
Cdd:PRK00409 513 EDKEKLNELIASLEELERE-LEQKAEEAEALLKEAEKLKEELEEKKEKLQEEEDKLLeEAEKEAQQAiKEAKKEADEIIK 591
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 713 DLENTVKKLQ-DQKhdmEREIKTLHRRLRE-----------ESAEWRQFQA--------DLQTAVVIANDIKSEAQEEIG 772
Cdd:PRK00409 592 ELRQLQKGGYaSVK---AHELIEARKRLNKanekkekkkkkQKEKQEELKVgdevkylsLGQKGEVLSIPDDKEAIVQAG 668
|
170 180 190
....*....|....*....|....*....|
gi 1844083964 773 DLKRRLHEAQEknEKLTKELEEIKSRKQEE 802
Cdd:PRK00409 669 IMKMKVPLSDL--EKIQKPKKKKKKKPKTV 696
|
|
| COG4913 |
COG4913 |
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown]; |
658-804 |
2.96e-04 |
|
Uncharacterized conserved protein, contains a C-terminal ATPase domain [Function unknown];
Pssm-ID: 443941 [Multi-domain] Cd Length: 1089 Bit Score: 44.91 E-value: 2.96e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 658 AKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLII--SDLENTVKKLQDQKHDMEREIKTL 735
Cdd:COG4913 608 NRAKLAALEAELAELEEELAEAEERLEALEAELDALQERREALQRLAEYSWDEIdvASAEREIAELEAELERLDASSDDL 687
|
90 100 110 120 130 140
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083964 736 hRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:COG4913 688 -AALEEQLEELEAELEELEEE-------LDELKGEIGRLEKELEQAEEELDELQDRLEAAEDLARLELR 748
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
408-659 |
3.07e-04 |
|
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: 44.37 E-value: 3.07e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 408 HSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhisyvIDEDVKsgr 487
Cdd:COG4942 16 AAQADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAA------LEAELA--- 86
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 488 ymELEQRYMDLAENARFEREQLlgvQQHLSNTLKMAEQDNKE---AQEMIGALKERSHHMERIIESEQKGKAALAATLEE 564
Cdd:COG4942 87 --ELEKEIAELRAELEAQKEEL---AELLRALYRLGRQPPLAlllSPEDFLDAVRRLQYLKYLAPARREQAEELRADLAE 161
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 565 YKATVASDQIEMNRLKAQLENEKQKVAELysihnSGDKSDIQDLLESVRLDKEKAETLASSLQEdlahtrnDANRLQDAI 644
Cdd:COG4942 162 LAALRAELEAERAELEALLAELEEERAAL-----EALKAERQKLLARLEKELAELAAELAELQQ-------EAEELEALI 229
|
250
....*....|....*
gi 1844083964 645 AKVEDEYRAFQEEAK 659
Cdd:COG4942 230 ARLEAEAAAAAERTP 244
|
|
| Spc7 |
smart00787 |
Spc7 kinetochore protein; This domain is found in cell division proteins which are required ... |
575-725 |
3.40e-04 |
|
Spc7 kinetochore protein; This domain is found in cell division proteins which are required for kinetochore-spindle association.
Pssm-ID: 197874 [Multi-domain] Cd Length: 312 Bit Score: 43.85 E-value: 3.40e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVrldKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYraf 654
Cdd:smart00787 155 GLKEDYKLLMKELELLNSI--------KPKLRDRKDAL---EEELRQLKQLEDELEDCDPTELDRAKEKLKKLLQEI--- 220
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083964 655 qEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRavkLHDNLIISDLENTVKKLQDQK 725
Cdd:smart00787 221 -MIKVKKLEELEEELQELESKIEDLTNKKSELNTEIAEAEKKLEQCR---GFTFKEIEKLKEQLKLLQSLT 287
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
513-806 |
3.58e-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: 44.81 E-value: 3.58e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 513 QQH---LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQK-------GKAALAATLEEYKATVASDQIEMNRLKAQ 582
Cdd:pfam10174 323 KQHievLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKqlqdlteEKSTLAGEIRDLKDMLDVKERKINVLQKK 402
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 583 LENEKQKVAElysihNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQI 662
Cdd:pfam10174 403 IENLQEQLRD-----KDKQLAGLKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREREDRERLEELESLKKEN 477
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 663 EDLNMTLEKLRSDLDEKETERSDMKE--------------TIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQ---- 724
Cdd:pfam10174 478 KDLKEKVSALQPELTEKESSLIDLKEhasslassglkkdsKLKSLEIAVEQKKEE-------CSKLENQLKKAHNAeeav 550
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 725 --KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDI---KSEAQEEIGDLKRRlheAQEKNEKLTKELEEIKSRK 799
Cdd:pfam10174 551 rtNPEINDRIRLLEQEVARYKEESGKAQAEVERLLGILREVeneKNDKDKKIAELESL---TLRQMKEQNKKVANIKHGQ 627
|
....*..
gi 1844083964 800 QEEERGR 806
Cdd:pfam10174 628 QEMKKKG 634
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
651-801 |
3.59e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 44.66 E-value: 3.59e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 651 YRAFQEEAKKQIEDLNMTLEK-------LRSDLD------EKETERSDMKETIFELEDEVEQHRAVKLHDNLiiSDLENT 717
Cdd:TIGR02168 170 YKERRKETERKLERTRENLDRledilneLERQLKslerqaEKAERYKELKAELRELELALLVLRLEELREEL--EELQEE 247
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 718 VKKLQDQKHDMEREIKTLH---RRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:TIGR02168 248 LKEAEEELEELTAELQELEeklEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILRERLANLERQLEELEAQLEE 327
|
....*..
gi 1844083964 795 IKSRKQE 801
Cdd:TIGR02168 328 LESKLDE 334
|
|
| EzrA |
pfam06160 |
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like ... |
520-803 |
3.61e-04 |
|
Septation ring formation regulator, EzrA; During the bacterial cell cycle, the tubulin-like cell-division protein FtsZ polymerizes into a ring structure that establishes the location of the nascent division site. EzrA modulates the frequency and position of FtsZ ring formation. The structure contains 5 spectrin like alpha helical repeats.
Pssm-ID: 428797 [Multi-domain] Cd Length: 542 Bit Score: 44.46 E-value: 3.61e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 520 LKMAEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAATLEEYKAtvASDQIEMNR---------LKAQLENE 586
Cdd:pfam06160 81 FKKAKKALDEIEELLDDIEEDIKQIleelDELLESEEKNREEVEELKDKYRE--LRKTLLANRfsygpaideLEKQLAEI 158
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 587 KQKVAELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDanrLQDAIAKVEDEYRAFQEE--------- 657
Cdd:pfam06160 159 EEEFSQFEELTESGDYLEAREVLEKLEEETDALEELMEDIPPLYEELKTE---LPDQLEELKEGYREMEEEgyalehlnv 235
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 658 ------AKKQIEDLNMTLEKLrsDLDEKETERSDMKETIFEL----EDEVEQHRAVKLHDNLIISDLENTVKKLQDQKHD 727
Cdd:pfam06160 236 dkeiqqLEEQLEENLALLENL--ELDEAEEALEEIEERIDQLydllEKEVDAKKYVEKNLPEIEDYLEHAEEQNKELKEE 313
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 728 MEREIKTLHrrLRE-ESAEWRQFQADLQTAV----VIANDIK------SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIk 796
Cdd:pfam06160 314 LERVQQSYT--LNEnELERVRGLEKQLEELEkrydEIVERLEekevaySELQEELEEILEQLEEIEEEQEEFKESLQSL- 390
|
....*..
gi 1844083964 797 sRKQEEE 803
Cdd:pfam06160 391 -RKDELE 396
|
|
| COG1340 |
COG1340 |
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown]; |
625-803 |
3.70e-04 |
|
Uncharacterized coiled-coil protein, contains DUF342 domain [Function unknown];
Pssm-ID: 440951 [Multi-domain] Cd Length: 297 Bit Score: 43.75 E-value: 3.70e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 625 SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR 701
Cdd:COG1340 5 ELSSSLEELEEKIEELREEIEELKEKRDELNEELKElaeKRDELNAQVKELREEAQELREKRDELNEKVKELKEERDELN 84
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 702 AVKlhdNLIISDLENtVKKLQDQKHDMEREIKTLHRRLREEsaEWRQfqadlQTAVVianDIKSEAQ--EEIGDLKRRLH 779
Cdd:COG1340 85 EKL---NELREELDE-LRKELAELNKAGGSIDKLRKEIERL--EWRQ-----QTEVL---SPEEEKElvEKIKELEKELE 150
|
170 180
....*....|....*....|....*...
gi 1844083964 780 EAQ---EKNEKLTKELEEIKS-RKQEEE 803
Cdd:COG1340 151 KAKkalEKNEKLKELRAELKElRKEAEE 178
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
655-825 |
3.79e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 44.37 E-value: 3.79e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 655 QEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVKLHdnliiSDLENTVKKLQDQKHDMEREIKT 734
Cdd:COG4717 76 LEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELPERLEE 150
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 735 LHRRLREesaeWRQFQADLQTAvviANDIKsEAQEEIGDLKRRLHEAQEKN-EKLTKELEEIKSRKQ--EEERGRVYNYM 811
Cdd:COG4717 151 LEERLEE----LRELEEELEEL---EAELA-ELQEELEELLEQLSLATEEElQDLAEELEELQQRLAelEEELEEAQEEL 222
|
170
....*....|....
gi 1844083964 812 NAVERDLAALRQGM 825
Cdd:COG4717 223 EELEEELEQLENEL 236
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
556-801 |
3.83e-04 |
|
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and four light chains it is a fundamental contractile protein found in all eukaryote cell types. This family consists of the coiled-coil myosin heavy chain tail region. The coiled-coil is composed of the tail from two molecules of myosin. These can then assemble into the macromolecular thick filament. The coiled-coil region provides the structural backbone the thick filament.
Pssm-ID: 460256 [Multi-domain] Cd Length: 1081 Bit Score: 44.78 E-value: 3.83e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 556 AALAATLEEYKATVASDQIEMNRLKAQLENEK-QKVAELYSIHN-SGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHT 633
Cdd:pfam01576 225 AELQAQIAELRAQLAKKEEELQAALARLEEETaQKNNALKKIRElEAQISELQEDLESERAARNKAEKQRRDLGEELEAL 304
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 634 RNDANRLQDAIAkVEDEYRAFQE----EAKKQIEDLNMTLEKLRSDLDEKETErsdmkeTIFELEDEVEQHRAVKlhdnl 709
Cdd:pfam01576 305 KTELEDTLDTTA-AQQELRSKREqevtELKKALEEETRSHEAQLQEMRQKHTQ------ALEELTEQLEQAKRNK----- 372
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 710 iiSDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND---IKSEAQE-------EIGDLKRRLH 779
Cdd:pfam01576 373 --ANLEKAKQALESENAELQAELRTLQQAKQDSEHKRKKLEGQLQELQARLSEserQRAELAEklsklqsELESVSSLLN 450
|
250 260
....*....|....*....|..
gi 1844083964 780 EAQEKNEKLTKELEEIKSRKQE 801
Cdd:pfam01576 451 EAEGKNIKLSKDVSSLESQLQD 472
|
|
| PRK09039 |
PRK09039 |
peptidoglycan -binding protein; |
575-676 |
5.37e-04 |
|
peptidoglycan -binding protein;
Pssm-ID: 181619 [Multi-domain] Cd Length: 343 Bit Score: 43.42 E-value: 5.37e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKAQLenekQKVAELYSIHNSGdKSDIQDLLESVRLDKEKAETLASSLQ---EDLAHTRNDANRLQDAIAKVEDEY 651
Cdd:PRK09039 54 ALDRLNSQI----AELADLLSLERQG-NQDLQDSVANLRASLSAAEAERSRLQallAELAGAGAAAEGRAGELAQELDSE 128
|
90 100
....*....|....*....|....*
gi 1844083964 652 RAFQEEAKKQIEDLNMTLEKLRSDL 676
Cdd:PRK09039 129 KQVSARALAQVELLNQQIAALRRQL 153
|
|
| 235kDa-fam |
TIGR01612 |
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in ... |
442-801 |
5.52e-04 |
|
reticulocyte binding/rhoptry protein; This model represents a group of paralogous families in plasmodium species alternately annotated as reticulocyte binding protein, 235-kDa family protein and rhoptry protein. Rhoptry protein is localized on the cell surface and is extremely large (although apparently lacking in repeat structure) and is important for the process of invasion of the RBCs by the parasite. These proteins are found in P. falciparum, P. vivax and P. yoelii.
Pssm-ID: 130673 [Multi-domain] Cd Length: 2757 Bit Score: 44.27 E-value: 5.52e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 442 KVIL--MESLCQQSDKLEHFSRqieyfRSLLDEHHISYVIDEDVKSGRYMELEQRYMDLAENARFEREQLLGVQQHLsnt 519
Cdd:TIGR01612 496 KLILmrMKDFKDIIDFMELYKP-----DEVPSKNIIGFDIDQNIKAKLYKEIEAGLKESYELAKNWKKLIHEIKKEL--- 567
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 520 lkmaEQDNKEAQEMIGALKERSHHMERIIEsEQKGKAALAATLEEyKATVASDQIEMNR----LKAQLENEKQKVAELYS 595
Cdd:TIGR01612 568 ----EEENEDSIHLEKEIKDLFDKYLEIDD-EIIYINKLKLELKE-KIKNISDKNEYIKkaidLKKIIENNNAYIDELAK 641
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 596 IH--------NSGDK--SDIQDLLESV---RLDKEKAEtLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQeeakkqi 662
Cdd:TIGR01612 642 ISpyqvpehlKNKDKiySTIKSELSKIyedDIDALYNE-LSSIVKENAIDNTEDKAKLDDLKSKIDKEYDKIQ------- 713
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 663 edlNMTLEKLRSDLDEKETERSDMKETIFELEDEVeqHRAVKLHDNLIISDLENTVKKLQDQKHDMEREIKTLHrRLREE 742
Cdd:TIGR01612 714 ---NMETATVELHLSNIENKKNELLDIIVEIKKHI--HGEINKDLNKILEDFKNKEKELSNKINDYAKEKDELN-KYKSK 787
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083964 743 SAEWRQFQADlqtAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:TIGR01612 788 ISEIKNHYND---QINIDNIKDEDAKQNYDKSKEYIKTISIKEDEIFKIINEMKFMKDD 843
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
538-804 |
5.92e-04 |
|
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: 43.96 E-value: 5.92e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 538 KERSHHMERIiESEQKGkAALAATLEEYKATVASDQIEMNRLKAQlENEKQKVaelysihnsgdksdIQDLLESVRLDKE 617
Cdd:pfam05557 21 MELEHKRARI-ELEKKA-SALKRQLDRESDRNQELQKRIRLLEKR-EAEAEEA--------------LREQAELNRLKKK 83
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 618 KAETLASSLQEDLAhTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELE--- 694
Cdd:pfam05557 84 YLEALNKKLNEKES-QLADAREVISCLKNELSELRRQIQRAELELQSTNSELEELQERLDLLKAKASEAEQLRQNLEkqq 162
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 695 ----------DEVEQHRAVKLHDNLIIsdleNTVKKLQDQKHDMEREIKtlhrRLREESAEWRQFQADlqtavviandiK 764
Cdd:pfam05557 163 sslaeaeqriKELEFEIQSQEQDSEIV----KNSKSELARIPELEKELE----RLREHNKHLNENIEN-----------K 223
|
250 260 270 280
....*....|....*....|....*....|....*....|...
gi 1844083964 765 SEAQEEIGDLKRRLH---EAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:pfam05557 224 LLLKEEVEDLKRKLEreeKYREEAATLELEKEKLEQELQSWVK 266
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
484-823 |
7.24e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 43.60 E-value: 7.24e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 484 KSGRYMELEQRYMDLAENARFEREQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIEseqkgKAALAATLE 563
Cdd:COG4717 61 PQGRKPELNLKELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQ-----LLPLYQELE 135
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 564 EYKATVASDQIEMNRLKAQLENEKQKVAELYSIhnsgdKSDIQDLLEsvRLDKEKAETLASSLQEdLAHTRNDANRLQDA 643
Cdd:COG4717 136 ALEAELAELPERLEELEERLEELRELEEELEEL-----EAELAELQE--ELEELLEQLSLATEEE-LQDLAEELEELQQR 207
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 644 IAKVEDEYrafqEEAKKQIEDLNMTLEKLRSDL-DEKETERSDMKETIFELEDEVEQHRAVKLHDN-------------- 708
Cdd:COG4717 208 LAELEEEL----EEAQEELEELEEELEQLENELeAAALEERLKEARLLLLIAAALLALLGLGGSLLsliltiagvlflvl 283
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 709 -LIISDLENTVKKLQDQKHDMErEIKTLHRRLREESAEWRQFQADLQTAvviandiKSEAQEEIGDLKRRLHEAQEKNEK 787
Cdd:COG4717 284 gLLALLFLLLAREKASLGKEAE-ELQALPALEELEEEELEELLAALGLP-------PDLSPEELLELLDRIEELQELLRE 355
|
330 340 350
....*....|....*....|....*....|....*.
gi 1844083964 788 LTKELEEIKSRKQEEERGRVYNYMNAveRDLAALRQ 823
Cdd:COG4717 356 AEELEEELQLEELEQEIAALLAEAGV--EDEEELRA 389
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
412-801 |
7.50e-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: 43.66 E-value: 7.50e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 412 EELQATLQELADLQQitqELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHhisyvideDVKSGRYMEL 491
Cdd:pfam10174 331 ESLTAKEQRAAILQT---EVDALRLRLEEKESFLNKKTKQLQDLTEEKSTLAGEIRDLKDML--------DVKERKINVL 399
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 492 EQRYMDLAENARFEREQLLGvqqhLSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKA----ALAATLEEYKA 567
Cdd:pfam10174 400 QKKIENLQEQLRDKDKQLAG----LKERVKSLQTDSSNTDTALTTLEEALSEKERIIERLKEQREredrERLEELESLKK 475
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 568 TVASDQIEMNRLKAQLENEKQKVAEL----YSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANR---- 639
Cdd:pfam10174 476 ENKDLKEKVSALQPELTEKESSLIDLkehaSSLASSGLKKDSKLKSLEIAVEQKKEECSKLENQLKKAHNAEEAVRtnpe 555
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 640 LQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRsdldEKETERSDMKETIFELEDEVEQHravklhdnliISDLENTVK 719
Cdd:pfam10174 556 INDRIRLLEQEVARYKEESGKAQAEVERLLGILR----EVENEKNDKDKKIAELESLTLRQ----------MKEQNKKVA 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 720 KLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSeaQEEIGDLKRRLHEAQ----EKNEKLT------ 789
Cdd:pfam10174 622 NIKHGQQEMKKKGAQLLEEARRREDNLADNSQQLQLEELMGALEKT--RQELDATKARLSSTQqslaEKDGHLTnlraer 699
|
410
....*....|...
gi 1844083964 790 -KELEEIKSRKQE 801
Cdd:pfam10174 700 rKQLEEILEMKQE 712
|
|
| DUF3584 |
pfam12128 |
Protein of unknown function (DUF3584); This protein is found in bacteria and eukaryotes. ... |
505-792 |
8.64e-04 |
|
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: 43.67 E-value: 8.64e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 505 EREQLLGVQQHlSNTLKMAEQdnkEAQEMIGALKErshhMERIIESEQKgkaALAATLEEYKATVASDQIEMNRLKAQLE 584
Cdd:pfam12128 239 IRPEFTKLQQE-FNTLESAEL---RLSHLHFGYKS----DETLIASRQE---ERQETSAELNQLLRTLDDQWKEKRDELN 307
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 585 NEKQKVAELYSihnsGDKSDIqDLLES--VRLDKEKAETLASSlQEDLAHTRNDANR-------LQDAIAKVEDEYRAFQ 655
Cdd:pfam12128 308 GELSAADAAVA----KDRSEL-EALEDqhGAFLDADIETAAAD-QEQLPSWQSELENleerlkaLTGKHQDVTAKYNRRR 381
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 656 ----EEAKKQIEDLNMTLEKLRSDLD-EKETERSDMKETIFELEDEVEQH-RAVKLHDNLIISDLE------NTVKKLQD 723
Cdd:pfam12128 382 skikEQNNRDIAGIKDKLAKIREARDrQLAVAEDDLQALESELREQLEAGkLEFNEEEYRLKSRLGelklrlNQATATPE 461
|
250 260 270 280 290 300
....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083964 724 QKHDMEREIKTLHRrLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKEL 792
Cdd:pfam12128 462 LLLQLENFDERIER-AREEQEAANAEVERLQSELRQARKRRDQASEALRQASRRLEERQSALDELELQL 529
|
|
| PRK12704 |
PRK12704 |
phosphodiesterase; Provisional |
616-792 |
8.94e-04 |
|
phosphodiesterase; Provisional
Pssm-ID: 237177 [Multi-domain] Cd Length: 520 Bit Score: 43.23 E-value: 8.94e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 616 KEKAETLASSLQEDLAHTRNDANR-----LQDAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:PRK12704 26 KKIAEAKIKEAEEEAKRILEEAKKeaeaiKKEALLEAKEEIHKLRNEFEKELRERRNELQKLEKRLLQKEENLDRKLELL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 691 FELEDEVEQHRAvklhdnlIISDLENTVKKLqdqkhdmEREIKTLHRRLREESAEWRQFQADLQTAVVIANdIKSEAQEE 770
Cdd:PRK12704 106 EKREEELEKKEK-------ELEQKQQELEKK-------EEELEELIEEQLQELERISGLTAEEAKEILLEK-VEEEARHE 170
|
170 180
....*....|....*....|...
gi 1844083964 771 IGDLKRRLH-EAQEKNEKLTKEL 792
Cdd:PRK12704 171 AAVLIKEIEeEAKEEADKKAKEI 193
|
|
| PRK10884 |
PRK10884 |
SH3 domain-containing protein; Provisional |
727-784 |
8.94e-04 |
|
SH3 domain-containing protein; Provisional
Pssm-ID: 182809 [Multi-domain] Cd Length: 206 Bit Score: 41.95 E-value: 8.94e-04
10 20 30 40 50
....*....|....*....|....*....|....*....|....*....|....*...
gi 1844083964 727 DMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEK 784
Cdd:PRK10884 97 DLENQVKTLTDKLNNIDNTWNQRTAEMQQKVAQSDSVINGLKEENQKLKNQLIVAQKK 154
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
708-804 |
9.09e-04 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 43.28 E-value: 9.09e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 708 NLIISDLENTVKKLQDQKHDME---REIKTLHRRLREESAEWRQ-FQADLQTAVVIANDIKSEAQEEIGDLKRRL----- 778
Cdd:PRK00409 519 NELIASLEELERELEQKAEEAEallKEAEKLKEELEEKKEKLQEeEDKLLEEAEKEAQQAIKEAKKEADEIIKELrqlqk 598
|
90 100 110
....*....|....*....|....*....|....
gi 1844083964 779 --------HEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:PRK00409 599 ggyasvkaHELIEARKRLNKANEKKEKKKKKQKE 632
|
|
| PTZ00108 |
PTZ00108 |
DNA topoisomerase 2-like protein; Provisional |
575-957 |
1.04e-03 |
|
DNA topoisomerase 2-like protein; Provisional
Pssm-ID: 240271 [Multi-domain] Cd Length: 1388 Bit Score: 43.50 E-value: 1.04e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 575 EMNRLKAQLENEKQKVAELYS----IHNSGDKSDIQDL--LESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVE 648
Cdd:PTZ00108 1003 KLERELARLSNKVRFIKHVINgelvITNAKKKDLVKELkkLGYVRFKDIIKKKSEKITAEEEEGAEEDDEADDEDDEEEL 1082
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 649 DEYRAFQEEAKKQIEDLNMT-LEKLRSDLDEKETERSDMKETifeledEVEQhravklhdnLIISDLENTVKKLQDQKHD 727
Cdd:PTZ00108 1083 GAAVSYDYLLSMPIWSLTKEkVEKLNAELEKKEKELEKLKNT------TPKD---------MWLEDLDKFEEALEEQEEV 1147
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 728 MEREIKTlHRRLREesaewRQFQADLQTAVVIANDIKSEAQEEIGDLKRrlhEAQEKNEKLTKELEEIKSRKQEEERGRV 807
Cdd:PTZ00108 1148 EEKEIAK-EQRLKS-----KTKGKASKLRKPKLKKKEKKKKKSSADKSK---KASVVGNSKRVDSDEKRKLDDKPDNKKS 1218
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 808 YNYMNAVERDLAALRQGMGLS--RRSSTSSEPTPTVKTLIKSFDSASQVPNPAAAAIPRTPLSPSPMKTPPAAAvspmqr 885
Cdd:PTZ00108 1219 NSSGSDQEDDEEQKTKPKKSSvkRLKSKKNNSSKSSEDNDEFSSDDLSKEGKPKNAPKRVSAVQYSPPPPSKRP------ 1292
|
330 340 350 360 370 380 390
....*....|....*....|....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 886 HSISGPISTSKPLTALSDKRPNygeipvqEHLLRTSSASRPASLPRVPAMES-AKTLSVSRRSSEEVKRDISA 957
Cdd:PTZ00108 1293 DGESNGGSKPSSPTKKKVKKRL-------EGSLAALKKKKKSEKKTARKKKSkTRVKQASASQSSRLLRRPRK 1358
|
|
| Filament |
pfam00038 |
Intermediate filament protein; |
597-825 |
1.05e-03 |
|
Intermediate filament protein;
Pssm-ID: 459643 [Multi-domain] Cd Length: 313 Bit Score: 42.60 E-value: 1.05e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 597 HNSGDKSDIQDLLE----SVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQI---EDLNMTL 669
Cdd:pfam00038 26 QNKLLETKISELRQkkgaEPSRLYSLYEKEIEDLRRQLDTLTVERARLQLELDNLRLAAEDFRQKYEDELnlrTSAENDL 105
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 670 EKLRSDLDEKETERSDMKETIFELEDEVEQHRavKLHDNLIiSDLENTVKKLQDQ-------KHDME---REIKTLH--- 736
Cdd:pfam00038 106 VGLRKDLDEATLARVDLEAKIESLKEELAFLK--KNHEEEV-RELQAQVSDTQVNvemdaarKLDLTsalAEIRAQYeei 182
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 737 -RRLREESAEWRQFQ-ADLQTAVVIANDIKSEAQEEIGDLKRRLH------EAQEK-NEKLTKELEEIKSRkQEEERGRV 807
Cdd:pfam00038 183 aAKNREEAEEWYQSKlEELQQAAARNGDALRSAKEEITELRRTIQsleielQSLKKqKASLERQLAETEER-YELQLADY 261
|
250
....*....|....*...
gi 1844083964 808 YNYMNAVERDLAALRQGM 825
Cdd:pfam00038 262 QELISELEAELQETRQEM 279
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
396-803 |
1.16e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 43.03 E-value: 1.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQ---QITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDE 472
Cdd:TIGR00618 206 LTLCTPCMPDTYHERKQVLEKELKHLREALqqtQQSHAYLTQKREAQEEQLKKQQLLKQLRARIEELRAQEAVLEETQER 285
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 473 -----------HHISYVIDEDVKSGRYMELEQRYMDLAENARFER------EQLLGVQQHLSNTLKMAEQDNKEAQE--- 532
Cdd:TIGR00618 286 inrarkaaplaAHIKAVTQIEQQAQRIHTELQSKMRSRAKLLMKRaahvkqQSSIEEQRRLLQTLHSQEIHIRDAHEvat 365
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 533 MIGALKERSHHMERIIESEQKGKAALAATLEEYKAtvasdqiemnrLKAQLENEKQKVAELYSIHNSgDKSDIQDLLESV 612
Cdd:TIGR00618 366 SIREISCQQHTLTQHIHTLQQQKTTLTQKLQSLCK-----------ELDILQREQATIDTRTSAFRD-LQGQLAHAKKQQ 433
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 613 RLDKEKAETLASSLQedlahtrndaNRLQDAIAKVEDEYRAFQeeAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFE 692
Cdd:TIGR00618 434 ELQQRYAELCAAAIT----------CTAQCEKLEKIHLQESAQ--SLKEREQQLQTKEQIHLQETRKKAVVLARLLELQE 501
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 693 LEDEVEQ---HRAVKLHDNLI-------ISDLENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIAND 762
Cdd:TIGR00618 502 EPCPLCGsciHPNPARQDIDNpgpltrrMQRGEQTYAQLETSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNR 581
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1844083964 763 IKSEAQ--EEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEE 803
Cdd:TIGR00618 582 SKEDIPnlQNITVRLQDLTEKLSEAEDMLACEQHALLRKLQPE 624
|
|
| PHA03247 |
PHA03247 |
large tegument protein UL36; Provisional |
828-967 |
1.32e-03 |
|
large tegument protein UL36; Provisional
Pssm-ID: 223021 [Multi-domain] Cd Length: 3151 Bit Score: 43.00 E-value: 1.32e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 828 SRRSSTSSEPTPTVKTLIKSF----DSASQVPNPAAAAIPRT----PLSPSPMKTPPAAAVSPMQRHSISGPISTSKPLT 899
Cdd:PHA03247 2878 PARPPVRRLARPAVSRSTESFalppDQPERPPQPQAPPPPQPqpqpPPPPQPQPPPPPPPRPQPPLAPTTDPAGAGEPSG 2957
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|.
gi 1844083964 900 ALSDKRPNY---GEIPVQEHLLRTSSASRPASLPRVPameSAKTLSVSRRSSEEVKRDISAQEGASPASLM 967
Cdd:PHA03247 2958 AVPQPWLGAlvpGRVAVPRFRVPQPAPSREAPASSTP---PLTGHSLSRVSSWASSLALHEETDPPPVSLK 3025
|
|
| PRK04778 |
PRK04778 |
septation ring formation regulator EzrA; Provisional |
490-796 |
1.86e-03 |
|
septation ring formation regulator EzrA; Provisional
Pssm-ID: 179877 [Multi-domain] Cd Length: 569 Bit Score: 42.13 E-value: 1.86e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 490 ELEQRYMDLAEN--ARFErEQLLGVQQhLSNTLKM--AEQDNKEAQEMIGALKERSHHM----ERIIESEQKGKAALAAT 561
Cdd:PRK04778 68 EWRQKWDEIVTNslPDIE-EQLFEAEE-LNDKFRFrkAKHEINEIESLLDLIEEDIEQIleelQELLESEEKNREEVEQL 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 562 LEEY---KATV---------ASDQIEmnrlkAQLENEKQKVAELYSIHNSGDKsdiqdllesvrldkEKAETLASSLQED 629
Cdd:PRK04778 146 KDLYrelRKSLlanrfsfgpALDELE-----KQLENLEEEFSQFVELTESGDY--------------VEAREILDQLEEE 206
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 630 LAHTRNDANRLQDAIAKVEDEYRAfqeeakkQIEDLNMTLEKLRSD---LDEKetersDMKETIFELEDEVEQHRAvklh 706
Cdd:PRK04778 207 LAALEQIMEEIPELLKELQTELPD-------QLQELKAGYRELVEEgyhLDHL-----DIEKEIQDLKEQIDENLA---- 270
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 707 dnlIISDLEntVKKLQDQKHDMEREIKTLHRRLREEsaewrqfqadlqtavVIAndiKSEAQEEIGDLKRRLHEAQEKNE 786
Cdd:PRK04778 271 ---LLEELD--LDEAEEKNEEIQERIDQLYDILERE---------------VKA---RKYVEKNSDTLPDFLEHAKEQNK 327
|
330
....*....|
gi 1844083964 787 KLTKELEEIK 796
Cdd:PRK04778 328 ELKEEIDRVK 337
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
516-799 |
1.90e-03 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 42.31 E-value: 1.90e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 516 LSNTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVaelys 595
Cdd:TIGR04523 396 LESKIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLKETIIKNNSEIKDLTNQDSVKELIIKNLDNTRESLETQL----- 470
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 596 ihnsgdkSDIQDLLESVRLDKEKaetlassLQEDLAHTRNDANRLQDAIAKVEDEyrafQEEAKKQIEDLNMTLEKLRSD 675
Cdd:TIGR04523 471 -------KVLSRSINKIKQNLEQ-------KQKELKSKEKELKKLNEEKKELEEK----VKDLTKKISSLKEKIEKLESE 532
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 676 LDEKETERSDMKETIFELEDeveqhravklhdnliisdlENTVKKLQDQKHDMEREIKTLHRRLREESAEWRQFQADLQT 755
Cdd:TIGR04523 533 KKEKESKISDLEDELNKDDF-------------------ELKKENLEKEIDEKNKEIEELKQTQKSLKKKQEEKQELIDQ 593
|
250 260 270 280
....*....|....*....|....*....|....*....|....*..
gi 1844083964 756 AVVIANDIKSEAQEE---IGDLKRRLHEAQEKNEKLTKELEEIKSRK 799
Cdd:TIGR04523 594 KEKEKKDLIKEIEEKekkISSLEKELEKAKKENEKLSSIIKNIKSKK 640
|
|
| GumC |
COG3206 |
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis]; |
607-823 |
2.00e-03 |
|
Exopolysaccharide export protein/domain GumC/Wzc1 [Cell wall/membrane/envelope biogenesis];
Pssm-ID: 442439 [Multi-domain] Cd Length: 687 Bit Score: 42.31 E-value: 2.00e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 607 DLLESVRLDKEKAETLASSLQEDLAHTR-------------NDANRLQDAIAKVEDEYRAFQ-----EEAKKQIEDLNMT 668
Cdd:COG3206 104 NLDEDPLGEEASREAAIERLRKNLTVEPvkgsnvieisytsPDPELAAAVANALAEAYLEQNlelrrEEARKALEFLEEQ 183
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 669 LEKLRSDLDEKETERSDMKET--IFELEDEVEQHRAvklhdnlIISDLENTVKKLQDQKhdmeREIKTLHRRLREESAEW 746
Cdd:COG3206 184 LPELRKELEEAEAALEEFRQKngLVDLSEEAKLLLQ-------QLSELESQLAEARAEL----AEAEARLAALRAQLGSG 252
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083964 747 RQFQADLQTAVVIANDIK--SEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERgrvyNYMNAVERDLAALRQ 823
Cdd:COG3206 253 PDALPELLQSPVIQQLRAqlAELEAELAELSARYTPNHPDVIALRAQIAALRAQLQQEAQ----RILASLEAELEALQA 327
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
398-665 |
2.24e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 42.25 E-value: 2.24e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 398 ERIHQMEENQHSTSEELQATLQEL-ADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHfSRQIEYFRSLL 470
Cdd:PRK04863 424 ERAKQLCGLPDLTADNAEDWLEEFqAKEQEATEELLSLEQKLSVAQAAHsqfeqaYQLVRKIAGEVSR-SEAWDVARELL 502
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 471 DEHhisyvidedvksgrymeleqrymdlaENARFEREQLLGVQQHLSnTLKMAEQDNKEAQEMIGALKERSHHMERIIES 550
Cdd:PRK04863 503 RRL--------------------------REQRHLAEQLQQLRMRLS-ELEQRLRQQQRAERLLAEFCKRLGKNLDDEDE 555
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 551 EQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSI----HNSgdksdiQDLLEsvRLDKEKAETLASSl 626
Cdd:PRK04863 556 LEQLQEELEARLESLSESVSEARERRMALRQQLEQLQARIQRLAARapawLAA------QDALA--RLREQSGEEFEDS- 626
|
250 260 270
....*....|....*....|....*....|....*....
gi 1844083964 627 qEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKQIEDL 665
Cdd:PRK04863 627 -QDVTEYMQQLLERERELTVERDELAARKQALDEEIERL 664
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
398-804 |
2.50e-03 |
|
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major component of the transverse filaments of the synaptonemal complex. Synaptonemal complexes are structures that are formed between homologous chromosomes during meiotic prophase.
Pssm-ID: 114219 [Multi-domain] Cd Length: 787 Bit Score: 42.02 E-value: 2.50e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 398 ERIHQMEENQHSTSEELQATLQE----LADLQQITQELNSENERLG---EEKVILMESLCQQSDKLEHFSRQIEYFRSLL 470
Cdd:pfam05483 88 EKIKKWKVSIEAELKQKENKLQEnrkiIEAQRKAIQELQFENEKVSlklEEEIQENKDLIKENNATRHLCNLLKETCARS 167
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 471 DEHHISYVIDEDVKSGRYMELEQRYMDL----------AENARFEREQLLGVQ----QHLSNTLKmAEQDNKEaqemiga 536
Cdd:pfam05483 168 AEKTKKYEYEREETRQVYMDLNNNIEKMilafeelrvqAENARLEMHFKLKEDhekiQHLEEEYK-KEINDKE------- 239
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 537 lKERSHHMERIIESEQKGKAaLAATLEEYKATV----ASDQIEMNRLKAQLENEKQKVAELYSIHNSGDKS--------- 603
Cdd:pfam05483 240 -KQVSLLLIQITEKENKMKD-LTFLLEESRDKAnqleEKTKLQDENLKELIEKKDHLTKELEDIKMSLQRSmstqkalee 317
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 604 DIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKK---QIEDLNMTLEKLRSDLDE-- 678
Cdd:pfam05483 318 DLQIATKTICQLTEEKEAQMEELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKnedQLKIITMELQKKSSELEEmt 397
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 679 -----KETERSDMKETIFELEDEVEQHRAV-KLHDNLIISDLENT--VKKLQDQKHDMEREIKTLHRRLREESAEWRQFQ 750
Cdd:pfam05483 398 kfknnKEVELEELKKILAEDEKLLDEKKQFeKIAEELKGKEQELIflLQAREKEIHDLEIQLTAIKTSEEHYLKEVEDLK 477
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 1844083964 751 ADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEER 804
Cdd:pfam05483 478 TELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQEDIINCKKQEER 531
|
|
| rad50 |
TIGR00606 |
rad50; All proteins in this family for which functions are known are involvedin recombination, ... |
134-817 |
2.52e-03 |
|
rad50; All proteins in this family for which functions are known are involvedin recombination, recombinational repair, and/or non-homologous end joining.They are components of an exonuclease complex with MRE11 homologs. This family is distantly related to the SbcC family of bacterial proteins.This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University).
Pssm-ID: 129694 [Multi-domain] Cd Length: 1311 Bit Score: 41.96 E-value: 2.52e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 134 QSKKLPSAGQGANDMALAKRSRSRTATECDVRMS------KSKSDNQISDRAALEAKVKDLLTLAKTKDvEILHLRNELR 207
Cdd:TIGR00606 403 QEDEAKTAAQLCADLQSKERLKQEQADEIRDEKKglgrtiELKKEILEKKQEELKFVIKELQQLEGSSD-RILELDQELR 481
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 208 DMRAQLGINEDHSEGDEKSEKETIMAHQPTDVESTLLQLQEQNTAIREELNQLKNENRMLKDRLNAlgfslEQRLDNsek 287
Cdd:TIGR00606 482 KAERELSKAEKNSLTETLKKEVKSLQNEKADLDRKLRKLDQEMEQLNHHTTTRTQMEMLTKDKMDK-----DEQIRK--- 553
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 288 lfgyqslspeitpgNQSDGGGTLTSSVeGSAPGSvedllSQDENTLmdHQHSNSMDNLDSECSEVYQPLTSSDDALDAPS 367
Cdd:TIGR00606 554 --------------IKSRHSDELTSLL-GYFPNK-----KQLEDWL--HSKSKEINQTRDRLAKLNKELASLEQNKNHIN 611
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 368 SSEsegipsiERSRKGSSGNASEVSVACLTErihQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKvilmE 447
Cdd:TIGR00606 612 NEL-------ESKEEQLSSYEDKLFDVCGSQ---DEESDLERLKEEIEKSSKQRAMLAGATAVYSQFITQLTDEN----Q 677
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 448 SLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKSGRYMELEQRymdlaenarfeREQLLGVQQHLSNTLKMAEQDN 527
Cdd:TIGR00606 678 SCCPVCQRVFQTEAELQEFISDLQSKLRLAPDKLKSTESELKKKEKR-----------RDEMLGLAPGRQSIIDLKEKEI 746
|
410 420 430 440 450 460 470 480
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 528 KEAQEMIGALKERSHHMERIIESEQKGKAALAATLEEYKaTVASDQIEMNRLKAQLENEKQKVAELYSIHNSGD------ 601
Cdd:TIGR00606 747 PELRNKLQKVNRDIQRLKNDIEEQETLLGTIMPEEESAK-VCLTDVTIMERFQMELKDVERKIAQQAAKLQGSDldrtvq 825
|
490 500 510 520 530 540 550 560
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 602 -----KSDIQDLLESVRLDKEKAETLASSLQEDLAHTRNDANRLQD---AIAKVEDEYRAFQEeakkQIEDLNMTLEKLR 673
Cdd:TIGR00606 826 qvnqeKQEKQHELDTVVSKIELNRKLIQDQQEQIQHLKSKTNELKSeklQIGTNLQRRQQFEE----QLVELSTEVQSLI 901
|
570 580 590 600 610 620 630 640
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 674 SDLDEKETERSDMKETIFELEDEVEQHRAVKLHDNLIISDLENTVKKLQDQKH-------------------DMEREIKT 734
Cdd:TIGR00606 902 REIKDAKEQDSPLETFLEKDQQEKEELISSKETSNKKAQDKVNDIKEKVKNIHgymkdienkiqdgkddylkQKETELNT 981
|
650 660 670 680 690 700 710 720
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 735 LHRRLREESAEWRQFQADLQTavvIANDIKSEAQEE--------IGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:TIGR00606 982 VNAQLEECEKHQEKINEDMRL---MRQDIDTQKIQErwlqdnltLRKRENELKEVEEELKQHLKEMGQMQVLQMKQEHQK 1058
|
730
....*....|.
gi 1844083964 807 VYNYMNAVERD 817
Cdd:TIGR00606 1059 LEENIDLIKRN 1069
|
|
| PRK01156 |
PRK01156 |
chromosome segregation protein; Provisional |
412-813 |
3.07e-03 |
|
chromosome segregation protein; Provisional
Pssm-ID: 100796 [Multi-domain] Cd Length: 895 Bit Score: 41.81 E-value: 3.07e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 412 EELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEHHI---------SYVIDED 482
Cdd:PRK01156 190 EKLKSSNLELENIKKQIADDEKSHSITLKEIERLSIEYNNAMDDYNNLKSALNELSSLEDMKNRyeseiktaeSDLSMEL 269
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 483 VKSGRYMELEQRYMDLAENARF-EREQLLGVQqhlsnTLKMAEQDNKEAQEMIGALKERSHHMERIIESEQKGKaalaat 561
Cdd:PRK01156 270 EKNNYYKELEERHMKIINDPVYkNRNYINDYF-----KYKNDIENKKQILSNIDAEINKYHAIIKKLSVLQKDY------ 338
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 562 leeykatvaSDQIEMNRLKAQLENEKQKVAELYSIHNSGDKSdIQDLLESVRLDKEKAETLASSLQEDLAHTRNDAnrlq 641
Cdd:PRK01156 339 ---------NDYIKKKSRYDDLNNQILELEGYEMDYNSYLKS-IESLKKKIEEYSKNIERMSAFISEILKIQEIDP---- 404
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 642 DAIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEKETE------RSDMKETIFELEDEVEQHravklhdnlIISDLE 715
Cdd:PRK01156 405 DAIKKELNEINVKLQDISSKVSSLNQRIRALRENLDELSRNmemlngQSVCPVCGTTLGEEKSNH---------IINHYN 475
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 716 NTVKKLQDQKHDMEREIKTLHRRLRE-ESAEWRQFQADLQTAVVIANDIKSeAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:PRK01156 476 EKKSRLEEKIREIEIEVKDIDEKIVDlKKRKEYLESEEINKSINEYNKIES-ARADLEDIKIKINELKDKHDKYEEIKNR 554
|
410
....*....|....*....
gi 1844083964 795 IKSRKQEEERGRVYNYMNA 813
Cdd:PRK01156 555 YKSLKLEDLDSKRTSWLNA 573
|
|
| Myosin_tail_1 |
pfam01576 |
Myosin tail; The myosin molecule is a multi-subunit complex made up of two heavy chains and ... |
404-806 |
3.16e-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: 41.70 E-value: 3.16e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 404 EENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSdklEHFSrQIEYFRSLLdehhisyvidedv 483
Cdd:pfam01576 4 EEEMQAKEEELQKVKERQQKAESELKELEKKHQQLCEEKNALQEQLQAET---ELCA-EAEEMRARL------------- 66
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 484 kSGRYMELEQRYMDLaeNARFEREQLLGVQQHlsntlkmaeQDNKEAQEMIGALKERSHHMERIIESEQKGKAALAA--- 560
Cdd:pfam01576 67 -AARKQELEEILHEL--ESRLEEEEERSQQLQ---------NEKKKMQQHIQDLEEQLDEEEAARQKLQLEKVTTEAkik 134
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 561 TLEEYKATVASDQIEMNRLKAQLEN-----------EKQKVAELYSIHNSGDK--SDIQDLL---ESVRLDKEKA----E 620
Cdd:pfam01576 135 KLEEDILLLEDQNSKLSKERKLLEEriseftsnlaeEEEKAKSLSKLKNKHEAmiSDLEERLkkeEKGRQELEKAkrklE 214
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 621 TLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQ----------EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETI 690
Cdd:pfam01576 215 GESTDLQEQIAELQAQIAELRAQLAKKEEELQAALarleeetaqkNNALKKIRELEAQISELQEDLESERAARNKAEKQR 294
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 691 FELEDEVEQHRAvKLHDNLiisDLENTVKKLQDQKhdmEREIKTLHRRLREESaewRQFQADLQ-------TAVVIANDI 763
Cdd:pfam01576 295 RDLGEELEALKT-ELEDTL---DTTAAQQELRSKR---EQEVTELKKALEEET---RSHEAQLQemrqkhtQALEELTEQ 364
|
410 420 430 440
....*....|....*....|....*....|....*....|...
gi 1844083964 764 KSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGR 806
Cdd:pfam01576 365 LEQAKRNKANLEKAKQALESENAELQAELRTLQQAKQDSEHKR 407
|
|
| PRK05771 |
PRK05771 |
V-type ATP synthase subunit I; Validated |
555-825 |
3.21e-03 |
|
V-type ATP synthase subunit I; Validated
Pssm-ID: 235600 [Multi-domain] Cd Length: 646 Bit Score: 41.45 E-value: 3.21e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 555 KAALAATLEEYKATVASDQ----IEMNRLKAQLENEK-QKVAELYSihnsgdksDIQDLLESVRLDKEKAETLAS----- 624
Cdd:PRK05771 8 KVLIVTLKSYKDEVLEALHelgvVHIEDLKEELSNERlRKLRSLLT--------KLSEALDKLRSYLPKLNPLREekkkv 79
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 625 ---SLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEaKKQIEDLNMTLEKLRS-DLDEKETERSDMKETIF-----ELED 695
Cdd:PRK05771 80 svkSLEELIKDVEEELEKIEKEIKELEEEISELENE-IKELEQEIERLEPWGNfDLDLSLLLGFKYVSVFVgtvpeDKLE 158
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 696 EVEQhrAVKLHDNLIISDLENT----VKKLQDQKHDMEREIKTLhrrlreesaEWRQFQAdlqtavviaNDIKSeAQEEI 771
Cdd:PRK05771 159 ELKL--ESDVENVEYISTDKGYvyvvVVVLKELSDEVEEELKKL---------GFERLEL---------EEEGT-PSELI 217
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 772 GDLKRRLHEAQEKNEKLTKELEEIKsRKQEEERGRVYNYM-NAVERDLAALRQGM 825
Cdd:PRK05771 218 REIKEELEEIEKERESLLEELKELA-KKYLEELLALYEYLeIELERAEALSKFLK 271
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
404-794 |
3.74e-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: 41.35 E-value: 3.74e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 404 EENQH--STSEELQATLQELADLQQITQELNSENERLGEEKVILM----ESLCQQSDKLEHFSRQIEYFRSLLDEhhisy 477
Cdd:pfam10174 67 EENQHlqLTIQALQDELRAQRDLNQLLQQDFTTSPVDGEDKFSTPelteENFRRLQSEHERQAKELFLLRKTLEE----- 141
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 478 videdvksgryMELEQRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGAlKERSHHMERIIESEQKGKA 556
Cdd:pfam10174 142 -----------MELRIETQKQTLGARDESiKKLLEMLQSKGLPKKSGEEDWERTRRIAEA-EMQLGHLEVLLDQKEKENI 209
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 557 ALAATLeEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdKSDIQDLLESVRLDKEKAETLASSLQEDL------ 630
Cdd:pfam10174 210 HLREEL-HRRNQLQPDPAKTKALQTVIEMKDTKISSL--------ERNIRDLEDEVQMLKTNGLLHTEDREEEIkqmevy 280
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 631 -AHT---RNDANRLQDAIAKVEDEYRAFQ----------EEAKKQIEDLNMTL--------------EKLRSDLDEKETE 682
Cdd:pfam10174 281 kSHSkfmKNKIDQLKQELSKKESELLALQtkletltnqnSDCKQHIEVLKESLtakeqraailqtevDALRLRLEEKESF 360
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 683 RSDMKETIFELEDE--VEQHRAVKLHDNLIISD-----LENTVKKLQDQKHDMEREIKTLHRR---LREESAEWRQFQAD 752
Cdd:pfam10174 361 LNKKTKQLQDLTEEksTLAGEIRDLKDMLDVKErkinvLQKKIENLQEQLRDKDKQLAGLKERvksLQTDSSNTDTALTT 440
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 753 LQTAVVIANDI-----------KSEAQEEIGDLKRRLHEAQEKNEKLTKELEE 794
Cdd:pfam10174 441 LEEALSEKERIierlkeqrereDRERLEELESLKKENKDLKEKVSALQPELTE 493
|
|
| PRK11637 |
PRK11637 |
AmiB activator; Provisional |
539-659 |
4.55e-03 |
|
AmiB activator; Provisional
Pssm-ID: 236942 [Multi-domain] Cd Length: 428 Bit Score: 40.83 E-value: 4.55e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 539 ERSHHMERII-------ESEQKGKAALAATLEEykatvasdqieMNRLKAQLENEKQKVAELYSihnsgDKSDIQDLLES 611
Cdd:PRK11637 149 EESQRGERILayfgylnQARQETIAELKQTREE-----------LAAQKAELEEKQSQQKTLLY-----EQQAQQQKLEQ 212
|
90 100 110 120 130
....*....|....*....|....*....|....*....|....*....|...
gi 1844083964 612 VRLDKEKAET-LASSLQED---LAHTRNDANRLQDAIAKVEDEYRAFQE-EAK 659
Cdd:PRK11637 213 ARNERKKTLTgLESSLQKDqqqLSELRANESRLRDSIARAEREAKARAErEAR 265
|
|
| PRK00409 |
PRK00409 |
recombination and DNA strand exchange inhibitor protein; Reviewed |
656-810 |
4.65e-03 |
|
recombination and DNA strand exchange inhibitor protein; Reviewed
Pssm-ID: 234750 [Multi-domain] Cd Length: 782 Bit Score: 40.97 E-value: 4.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 656 EEAKKQIEDLNMTLEKLRSDLDEKETErsdMKETIFELEDEVEQhrAVKLHDNL--IISDLENTVKKLqdqKHDMEREIK 733
Cdd:PRK00409 505 EEAKKLIGEDKEKLNELIASLEELERE---LEQKAEEAEALLKE--AEKLKEELeeKKEKLQEEEDKL---LEEAEKEAQ 576
|
90 100 110 120 130 140 150
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083964 734 TLHRRLREESAEWRQFQADLQTAVVIAndIKSEAQEEIgdlKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNY 810
Cdd:PRK00409 577 QAIKEAKKEADEIIKELRQLQKGGYAS--VKAHELIEA---RKRLNKANEKKEKKKKKQKEKQEELKVGDEVKYLSL 648
|
|
| mukB |
PRK04863 |
chromosome partition protein MukB; |
495-801 |
4.66e-03 |
|
chromosome partition protein MukB;
Pssm-ID: 235316 [Multi-domain] Cd Length: 1486 Bit Score: 41.10 E-value: 4.66e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 495 YMDLAENARFEREQLLGVQQHLSN---TLKMAEQDNKEAQEMIGALKERSHHMERIIESeQKGKAALAATLEEYKATVAS 571
Cdd:PRK04863 274 YMRHANERRVHLEEALELRRELYTsrrQLAAEQYRLVEMARELAELNEAESDLEQDYQA-ASDHLNLVQTALRQQEKIER 352
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 572 DQIEMNRLKAQLENEKQKVAElysihnsgdksdIQDLLESVRLDKEKAET----LASSL---QE--DLAHTR----NDAN 638
Cdd:PRK04863 353 YQADLEELEERLEEQNEVVEE------------ADEQQEENEARAEAAEEevdeLKSQLadyQQalDVQQTRaiqyQQAV 420
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 639 RLQD-----------AIAKVEDEYRAFQEEAKKQIEDLNMTLEKLRSDLDEK---------------ETERSDMKETIFE 692
Cdd:PRK04863 421 QALErakqlcglpdlTADNAEDWLEEFQAKEQEATEELLSLEQKLSVAQAAHsqfeqayqlvrkiagEVSRSEAWDVARE 500
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 693 LEDEVEQHRAvklhdnliisdlentvkkLQDQKHDMEREIKTLHRRLREESAEWR-------QFQADLQTAVViANDIKS 765
Cdd:PRK04863 501 LLRRLREQRH------------------LAEQLQQLRMRLSELEQRLRQQQRAERllaefckRLGKNLDDEDE-LEQLQE 561
|
330 340 350
....*....|....*....|....*....|....*.
gi 1844083964 766 EAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQE 801
Cdd:PRK04863 562 ELEARLESLSESVSEARERRMALRQQLEQLQARIQR 597
|
|
| MAD |
pfam05557 |
Mitotic checkpoint protein; This family consists of several eukaryotic mitotic checkpoint ... |
412-808 |
5.12e-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: 40.88 E-value: 5.12e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 412 EELQATLQELADLQQITQELNSENERLGEEKVIL------MESLCQQSDKLEHFSRQIEYFRSLLDEHHISYVIDEDVKs 485
Cdd:pfam05557 156 QNLEKQQSSLAEAEQRIKELEFEIQSQEQDSEIVknskseLARIPELEKELERLREHNKHLNENIENKLLLKEEVEDLK- 234
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 486 gRYMELEQRYMDLAENARFEREQLLG--------VQQH---------LSNTLKMAEQDNKEAQEMIGALKERSHHMERII 548
Cdd:pfam05557 235 -RKLEREEKYREEAATLELEKEKLEQelqswvklAQDTglnlrspedLSRRIEQLQQREIVLKEENSSLTSSARQLEKAR 313
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 549 -ESEQKGKAALAATLEEYKATVASDQI-------------EMNRLKAQLEN-EKQKVAELYSIHNSGDKSDIQDLLESVR 613
Cdd:pfam05557 314 rELEQELAQYLKKIEDLNKKLKRHKALvrrlqrrvllltkERDGYRAILESyDKELTMSNYSPQLLERIEEAEDMTQKMQ 393
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 614 LDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEdeyrafQEEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFEL 693
Cdd:pfam05557 394 AHNEEMEAQLSVAEEELGGYKQQAQTLERELQALR------QQESLADPSYSKEEVDSLRRKLETLELERQRLREQKNEL 467
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 694 EDEVEQH-----------RAVKLHDNliisdleNTVKKLQDQKHDMER---EIKTLHRRLreesaewRQFQADLQTAVVI 759
Cdd:pfam05557 468 EMELERRclqgdydpkktKVLHLSMN-------PAAEAYQQRKNQLEKlqaEIERLKRLL-------KKLEDDLEQVLRL 533
|
410 420 430 440
....*....|....*....|....*....|....*....|....*....
gi 1844083964 760 ANDIKSEAQEEIGDLKRRLHEAQEKNEKltkeLEEIKSRKQEEERGRVY 808
Cdd:pfam05557 534 PETTSTMNFKEVLDLRKELESAELKNQR----LKEVFQAKIQEFRDVCY 578
|
|
| 46 |
PHA02562 |
endonuclease subunit; Provisional |
507-736 |
5.42e-03 |
|
endonuclease subunit; Provisional
Pssm-ID: 222878 [Multi-domain] Cd Length: 562 Bit Score: 40.77 E-value: 5.42e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 507 EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKE--RSHHMEriIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLE 584
Cdd:PHA02562 195 QQIKTYNKNIEEQRKKNGENIARKQNKYDELVEeaKTIKAE--IEELTDELLNLVMDIEDPSAALNKLNTAAAKIKSKIE 272
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 585 NeKQKVAELYSIHN-----SGDKSDIQDLLESVrldKEKAETLASSLqedlahtrNDANRLQDAIAKVEDEYRafqeEAK 659
Cdd:PHA02562 273 Q-FQKVIKMYEKGGvcptcTQQISEGPDRITKI---KDKLKELQHSL--------EKLDTAIDELEEIMDEFN----EQS 336
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*..
gi 1844083964 660 KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIKTLH 736
Cdd:PHA02562 337 KKLLELKNKISTNKQSLITLVDKAKKVKAAIEELQAEFVDNAEE-------LAKLQDELDKIVKTKSELVKEKYHRG 406
|
|
| CH_MACF1_rpt2 |
cd21240 |
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, ... |
1012-1076 |
5.43e-03 |
|
second calponin homology (CH) domain found in microtubule-actin cross-linking factor 1, isoforms 1/2/3/5 (MACF1) and similar proteins; MACF1, also called 620 kDa actin-binding protein (ABP620), actin cross-linking family protein 7 (ACF7), macrophin-1, or trabeculin-alpha, is a large protein containing numerous spectrin and leucine-rich repeat (LRR) domains. It facilitates actin-microtubule interactions at the cell periphery and couples the microtubule network to cellular junctions. MACF1 contains two copies of the CH domain. This model corresponds to the second CH domain. CH domains are actin filament (F-actin) binding motifs.
Pssm-ID: 409089 Cd Length: 107 Bit Score: 37.71 E-value: 5.43e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 1012 SKRNALLKWCQKKTEGY---------------------------------------QRRNFMLAFQAAESVGIKSTLDIn 1052
Cdd:cd21240 4 SAKEKLLLWTQKVTAGYtgikctnfsscwsdgkmfnalihryrpdlvdmervqiqsNRENLEQAFEVAERLGVTRLLDA- 82
|
90 100
....*....|....*....|....
gi 1844083964 1053 EMVRTERPDWQNVMLYVTAIYKYF 1076
Cdd:cd21240 83 EDVDVPSPDEKSVITYVSSIYDAF 106
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
396-592 |
5.57e-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: 40.52 E-value: 5.57e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 396 LTERIHQMEENQHSTSEELQATLQELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDEhhi 475
Cdd:COG4942 32 LQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRAELEAQKEELAE--- 108
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 476 syVIDEDVKSGRYMELE--------------QRYMDLAENARFER-EQLLGVQQHLSNTLKMAEQDNKEAQEMIGALKER 540
Cdd:COG4942 109 --LLRALYRLGRQPPLAlllspedfldavrrLQYLKYLAPARREQaEELRADLAELAALRAELEAERAELEALLAELEEE 186
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 1844083964 541 SHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAE 592
Cdd:COG4942 187 RAALEALKAERQKLLARLEKELAELAAELAELQQEAEELEALIARLEAEAAA 238
|
|
| Prefoldin_2 |
pfam01920 |
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996. |
660-754 |
6.02e-03 |
|
Prefoldin subunit; This family includes prefoldin subunits that are not detected by pfam02996.
Pssm-ID: 396482 [Multi-domain] Cd Length: 102 Bit Score: 37.20 E-value: 6.02e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 660 KQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDeVEQHRAV--KLHDNLIISDLENTVKKLQDQKHDMEREIKTLHR 737
Cdd:pfam01920 2 NKFQQLQQQLQLLAQQIKQLETQLKELELALEELEL-LDEDTKVykLIGDVLVKQDKEEVKEQLEERKETLEKEIKTLEK 80
|
90
....*....|....*..
gi 1844083964 738 RLREESAEWRQFQADLQ 754
Cdd:pfam01920 81 QLEKLEKELEELKEELY 97
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
656-823 |
6.49e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 40.27 E-value: 6.49e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 656 EEAKKQIEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAVklhdnliISDLENTVKKLQDQKHDMEREIKtl 735
Cdd:COG4372 34 RKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQLEEE-------LEELNEQLQAAQAELAQAQEELE-- 104
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 736 hrRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVE 815
Cdd:COG4372 105 --SLQEEAEELQEELEELQKERQDLEQQRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQELQALSEAEAE 182
|
....*...
gi 1844083964 816 RDLAALRQ 823
Cdd:COG4372 183 QALDELLK 190
|
|
| sbcc |
TIGR00618 |
exonuclease SbcC; All proteins in this family for which functions are known are part of an ... |
419-778 |
6.63e-03 |
|
exonuclease SbcC; All proteins in this family for which functions are known are part of an exonuclease complex with sbcD homologs. This complex is involved in the initiation of recombination to regulate the levels of palindromic sequences in DNA. This family is based on the phylogenomic analysis of JA Eisen (1999, Ph.D. Thesis, Stanford University). [DNA metabolism, DNA replication, recombination, and repair]
Pssm-ID: 129705 [Multi-domain] Cd Length: 1042 Bit Score: 40.72 E-value: 6.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 419 QELADLQQITQELNSENERLGEEKVILMESLCQQSDKLEHFSRQIEYFRSLLDehhisyvideDVKSGRYMELEQRYMDL 498
Cdd:TIGR00618 542 TSEEDVYHQLTSERKQRASLKEQMQEIQQSFSILTQCDNRSKEDIPNLQNITV----------RLQDLTEKLSEAEDMLA 611
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 499 AENarfeREQLLGVQQHLSNTLKMAEQDNKEAQEmigALKERSHHMERIIESEQKGKAALAATLEEYKATVASDQiemnR 578
Cdd:TIGR00618 612 CEQ----HALLRKLQPEQDLQDVRLHLQQCSQEL---ALKLTALHALQLTLTQERVREHALSIRVLPKELLASRQ----L 680
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 579 LKAQLENEKQKVA---ELYSIHNSGDKSDIQDLLESVRLDKEKAETLASSLQE------DLAHTRNDANRLQDAI--AKV 647
Cdd:TIGR00618 681 ALQKMQSEKEQLTywkEMLAQCQTLLRELETHIEEYDREFNEIENASSSLGSDlaaredALNQSLKELMHQARTVlkART 760
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 648 EDEYRAFQEEAKKqiEDLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHR-----AVKLHDNLIISDLENTVKKLQ 722
Cdd:TIGR00618 761 EAHFNNNEEVTAA--LQTGAELSHLAAEIQFFNRLREEDTHLLKTLEAEIGQEIpsdedILNLQCETLVQEEEQFLSRLE 838
|
330 340 350 360 370
....*....|....*....|....*....|....*....|....*....|....*....
gi 1844083964 723 dQKHDMEREIKTLHRRLREES---AEWRQFQADLQTAVVIANDIKSEAQEEIGDLKRRL 778
Cdd:TIGR00618 839 -EKSATLGEITHQLLKYEECSkqlAQLTQEQAKIIQLSDKLNGINQIKIQFDGDALIKF 896
|
|
| PTZ00121 |
PTZ00121 |
MAEBL; Provisional |
517-804 |
7.75e-03 |
|
MAEBL; Provisional
Pssm-ID: 173412 [Multi-domain] Cd Length: 2084 Bit Score: 40.51 E-value: 7.75e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 517 SNTLKMAEQDNKEAQEMIGAlkERSHHMERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELYSI 596
Cdd:PTZ00121 1499 ADEAKKAAEAKKKADEAKKA--EEAKKADEAKKAEEAKKADEAKKAEEKKKADELKKAEELKKAEEKKKAEEAKKAEEDK 1576
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 597 HNSGDKSDiqdllESVRLDKEKAETLASSLQEDLAHTRNDANRLQDAIAKVEDEYRAfqEEAKKQIEDLNMTL--EKLRS 674
Cdd:PTZ00121 1577 NMALRKAE-----EAKKAEEARIEEVMKLYEEEKKMKAEEAKKAEEAKIKAEELKKA--EEEKKKVEQLKKKEaeEKKKA 1649
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 675 DLDEKETERSDMKETIFELEDEVEQHRAVKLHDNliisdlENTVKKLQDQ---KHDMEREIKTLHRRLREESAEWRQFQA 751
Cdd:PTZ00121 1650 EELKKAEEENKIKAAEEAKKAEEDKKKAEEAKKA------EEDEKKAAEAlkkEAEEAKKAEELKKKEAEEKKKAEELKK 1723
|
250 260 270 280 290
....*....|....*....|....*....|....*....|....*....|....*
gi 1844083964 752 DLQTAVVIANDIKSEAQEEigdlKRRLHEAQ--EKNEKLTKELEEIKSRKQEEER 804
Cdd:PTZ00121 1724 AEEENKIKAEEAKKEAEED----KKKAEEAKkdEEEKKKIAHLKKEEEKKAEEIR 1774
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
544-864 |
8.13e-03 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 39.89 E-value: 8.13e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 544 MERIIESEQKGKAALAATLEEYKATVASDQIEMNRLKAQLENEKQKVAELysihnsgdksdiQDLLESVRLDKEKAETLA 623
Cdd:COG4372 29 LSEQLRKALFELDKLQEELEQLREELEQAREELEQLEEELEQARSELEQL------------EEELEELNEQLQAAQAEL 96
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 624 SSLQEDLAHTRNDANRLQDAIAKVEDEYRAFQEEAKKqiedLNMTLEKLRSDLDEKETERSDMKETIFELEDEVEQHRAV 703
Cdd:COG4372 97 AQAQEELESLQEEAEELQEELEELQKERQDLEQQRKQ----LEAQIAELQSEIAEREEELKELEEQLESLQEELAALEQE 172
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 704 KLhdNLIISDLENTVKKLQDQ---------KHDMEREIKTLHRRLREESAEWRQFQADLQTAVVIANDIKSEAQEEIGDL 774
Cdd:COG4372 173 LQ--ALSEAEAEQALDELLKEanrnaekeeELAEAEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEE 250
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 1844083964 775 KRRLHEAQEKNEKLTKELEEIKSRKQEEERGRVYNYMNAVERDLAALRQGMGLSRRSSTSSEPTPTVKTLIKSFDSASQV 854
Cdd:COG4372 251 LLEEVILKEIEELELAILVEKDTEEEELEIAALELEALEEAALELKLLALLLNLAALSLIGALEDALLAALLELAKKLEL 330
|
330
....*....|
gi 1844083964 855 PNPAAAAIPR 864
Cdd:COG4372 331 ALAILLAELA 340
|
|
| |
