|
Name |
Accession |
Description |
Interval |
E-value |
| MRVI1 |
pfam05781 |
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the ... |
1056-1471 |
2.36e-114 |
|
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the lymphoid-restricted membrane protein (JAW1) and the IP3 receptor associated cGMP kinase substrates A and B (IRAGA and IRAGB). The function of MRVI1 is unknown although mutations in the Mrvi1 gene induces myeloid leukaemia by altering the expression of a gene important for myeloid cell growth and/or differentiation so it has been speculated that Mrvi1 is a tumour suppressor gene. IRAG is very similar in sequence to MRVI1 and is an essential NO/cGKI-dependent regulator of IP3-induced calcium release. Activation of cGKI decreases IP3-stimulated elevations in intracellular calcium, induces smooth muscle relaxation and contributes to the antiproliferative and pro-apoptotic effects of NO/cGMP. Jaw1 is a member of a class of proteins with COOH-terminal hydrophobic membrane anchors and is structurally similar to proteins involved in vesicle targeting and fusion. This suggests that the function and/or the structure of the ER in lymphocytes may be modified by lymphoid-restricted resident ER proteins.
Pssm-ID: 461738 Cd Length: 521 Bit Score: 370.76 E-value: 2.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1056 MQRSKFRKNLEHTQSMEAIEEHTPQEEQSDSTQNEVP--TESAANRNKSPNQdknifSPSEKEVETEFHRLSLGFKCDVF 1133
Cdd:pfam05781 118 LMRNKNLVGLEAPEESETAEQERKESAAGEDVMSSIPdvLVKKVNFHQSLNT-----SANEKEVEAEFLRLSLAFKCDWF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1134 TLEKRLRLEERSRDLAEENLKKEVKNCKGLLEKLAPLCEDDNQSLEIIQRLQKNFDVLVQSMSRVSNRSEMLGAIHQESR 1213
Cdd:pfam05781 193 TLEKRVKLEERSRDLAEENLKKEITNCLKLLESLTPLCEHDNQAQEIYKKLEKSIAVLSQCAARVASRAEMLGAINQESR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1214 VSKAVEVMIQHVENLKRMYTKEHAELLELKETLVQSERSFGSYSERDDLRNKKTSGSQYSKPSS-RRVSVPAISRNIGNA 1292
Cdd:pfam05781 273 VSKAVEVMIQHVENLKRMYAKEHAELEELKQLLLQNSRSFNPLEDEDDCQIKKRSMSLNSKPSSlRRVSIASLPRNIGNS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1293 SHFE-MPKLHEISEteadklcRTGNWRVMGMKQNSTRPTLQRFVSSCPWAESDEPSLMKGYEQESESPpaeekREEIVE- 1370
Cdd:pfam05781 353 GMASgMENNDRLSR-------RSSSWRILGNKQSEHRPSLHRFISTYSWSDAEEESCEVKAKDEEEPY-----GEEGVEk 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1371 -RKSSLTEMGIKISSVLMtSTTCDQISSRFADFRHSVSKSNRGMWISVVLTVLFAAFIGLIASFAFQPSVDAAPVGTGDS 1449
Cdd:pfam05781 421 tRKPSLSEKKNNPSKWDV-SSIYETLASWLTNLYPSLRKANKVLWLSVAAIVLFAALMSFLTGQFFQSCVEAAPTQEGDS 499
|
410 420
....*....|....*....|..
gi 972982496 1450 WVAIQQFLWPYTGLRHNGQPPV 1471
Cdd:pfam05781 500 WCSLEHILWPFTGLQHEGPPPV 521
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
342-532 |
4.07e-66 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 221.59 E-value: 4.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 342 LETSDLVYCVADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNME 421
Cdd:pfam14662 1 METSDLLTCVEDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 422 ENRARSVAQNKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQI 501
Cdd:pfam14662 81 EARRSLLAQNKQLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQI 160
|
170 180 190
....*....|....*....|....*....|.
gi 972982496 502 QELKSTIEEYSSVTDLLRAEKNKLESHVEML 532
Cdd:pfam14662 161 EELKSTVEEYSSIEEELRAEKSRLESQLPDM 191
|
|
| EF-hand_9 |
pfam14658 |
EF-hand domain; |
224-289 |
1.09e-17 |
|
EF-hand domain;
Pssm-ID: 405361 Cd Length: 66 Bit Score: 78.62 E-value: 1.09e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972982496 224 DTIFHACDTQRRGKVSVSRIVDYLRHTTSRESEDSGLEELCNMLDPEHRDISIDLETYHAIMREWI 289
Cdd:pfam14658 1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDALVDLDTFLRVMRDWI 66
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
367-806 |
3.45e-07 |
|
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: 55.11 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 367 KLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNnmeenraRSVAQNKQMERENQSLISKIA 446
Cdd:pfam05483 255 KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-------RSMSTQKALEEDLQIATKTIC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 447 SLQEENIKNMvdiDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKNKLE 526
Cdd:pfam05483 328 QLTEEKEAQM---EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 527 SHVEMLQPALGLDGMSL---SGAYRLNQSTTGSLQtELALAQQAPETpaavsmlaapyhapldETLDRDVFLLLQGPASE 603
Cdd:pfam05483 405 VELEELKKILAEDEKLLdekKQFEKIAEELKGKEQ-ELIFLLQAREK----------------EIHDLEIQLTAIKTSEE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 604 QNSAEFKAVVRKLHQDFREDICAVMCTLKRFTENHIESEDLREIWLKTMNSElEEKRNVWLQRVQLLDQYKcSLEEELIK 683
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ-EDIINCKKQEERMLKQIE-NLEEKEMN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 684 VASRLRRCRTEVAHLKKELSARLPELEAQRQMQGDDKLRARPERGLAEaaSQTESSAPQVADKSTAASLLWEDESLLRND 763
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE--NKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 972982496 764 LQDTLRE-----------RVSLQDNSQALALSCGQFEQRLEEKRVNEHTAVEPV 806
Cdd:pfam05483 624 GSAENKQlnayeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV 677
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-536 |
8.69e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 361 LQDEVRKLKLAVDtmeETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQS 440
Cdd:TIGR02169 693 LQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 441 LISKIASLQEE--NIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKN----------AQIQELKSTI 508
Cdd:TIGR02169 770 LEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqelqEQRIDLKEQI 849
|
170 180
....*....|....*....|....*...
gi 972982496 509 EEYSSVTDLLRAEKNKLESHVEMLQPAL 536
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAAL 877
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
352-561 |
4.07e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 352 ADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELktQAKSGQQSAMKEKL--LKGELEEMKVTLNNMEENRARSVA 429
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQL--QAAQAELAQAQEELesLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 430 QNKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELcavnaDLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIE 509
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 972982496 510 EYSSVTDLLRAEKNKLESHVEMLQPALGLDGMSLSGAYRLNQSTTGSLQTEL 561
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
458-775 |
1.18e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 458 DIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKNKLESHVEMLQpalg 537
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 538 ldgmslsgaYRLNQSTTGSLQTELALAQqapetpaavsmlaapyhapLDETLDRDVFLLlqgpasEQNSAEFkAVVRKLH 617
Cdd:TIGR02168 309 ---------ERLANLERQLEELEAQLEE-------------------LESKLDELAEEL------AELEEKL-EELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 618 QDFREdicavmctlkRFTENHIESEDLREIWlktmnselEEKRNVWLQRVQLLDQykcsLEEELIKVASRLRRCRTEVAH 697
Cdd:TIGR02168 354 ESLEA----------ELEELEAELEELESRL--------EELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972982496 698 LKKELSARLPELEAQRQmQGDDKLRARPERGLAEAASQTESSAPQVADKSTAASLLWEDESLLRNDLQDTLRERVSLQ 775
Cdd:TIGR02168 412 LEDRRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-782 |
1.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 363 DEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNmeenrARSVAQNKQMERENQSLI 442
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 443 SKIASLQEEniknMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVG-EKEALLCEKNAQIQELKSTIEEYSSVTDLLRAE 521
Cdd:COG4717 146 ERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 522 KNKLESHVEMLQPALGLDGM--SLSGAYRLNQSTTG--SLQTELALAQQAPETPAAVSMLAAPYHAPLDETLDRDVFLLL 597
Cdd:COG4717 222 LEELEEELEQLENELEAAALeeRLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 598 QGPASEQNSAEFKAVVRKLHQDFREDIcavmcTLKRFTENHIESEDLREIW-LKTMNSELEEKRNVWL------QRVQLL 670
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAAL-----GLPPDLSPEELLELLDRIEeLQELLREAEELEEELQleeleqEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 671 DQYKCSLEEELIKVASRLRRC---RTEVAHLKKELSARLPELEAQRQMQGDDKLRARpergLAEAASQTESSAPQVADKS 747
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEE----LEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....*..
gi 972982496 748 TA-ASLLWEDESLLRND-LQDTLRERVSLQDNSQALA 782
Cdd:COG4717 453 EElAELEAELEQLEEDGeLAELLQELEELKAELRELA 489
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
401-480 |
3.78e-04 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 42.49 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 401 MKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQSLISKI---ASLQEENIKNMVdiDHLQKKMAELcavNADLQ 477
Cdd:cd21759 72 RKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALIKKIktnDMITRKEIDKLY--NALVKKVDKQ---LAELQ 146
|
...
gi 972982496 478 MQV 480
Cdd:cd21759 147 KKL 149
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-536 |
5.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAK---SGQQSAMKEKLLKGELEEMKVTLNNMEENRARS 427
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 428 VAQNKQMERENQSLISKIASLQEenIKNmvDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEK----NAQIQE 503
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE--LKK--KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTpeklEKELEE 395
|
170 180 190
....*....|....*....|....*....|...
gi 972982496 504 LKSTIEEYSSVTDLLRAEKNKLESHVEMLQPAL 536
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| |
|
Name |
Accession |
Description |
Interval |
E-value |
| MRVI1 |
pfam05781 |
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the ... |
1056-1471 |
2.36e-114 |
|
MRVI1 protein; This family consists of mammalian MRVI1 proteins which are related to the lymphoid-restricted membrane protein (JAW1) and the IP3 receptor associated cGMP kinase substrates A and B (IRAGA and IRAGB). The function of MRVI1 is unknown although mutations in the Mrvi1 gene induces myeloid leukaemia by altering the expression of a gene important for myeloid cell growth and/or differentiation so it has been speculated that Mrvi1 is a tumour suppressor gene. IRAG is very similar in sequence to MRVI1 and is an essential NO/cGKI-dependent regulator of IP3-induced calcium release. Activation of cGKI decreases IP3-stimulated elevations in intracellular calcium, induces smooth muscle relaxation and contributes to the antiproliferative and pro-apoptotic effects of NO/cGMP. Jaw1 is a member of a class of proteins with COOH-terminal hydrophobic membrane anchors and is structurally similar to proteins involved in vesicle targeting and fusion. This suggests that the function and/or the structure of the ER in lymphocytes may be modified by lymphoid-restricted resident ER proteins.
Pssm-ID: 461738 Cd Length: 521 Bit Score: 370.76 E-value: 2.36e-114
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1056 MQRSKFRKNLEHTQSMEAIEEHTPQEEQSDSTQNEVP--TESAANRNKSPNQdknifSPSEKEVETEFHRLSLGFKCDVF 1133
Cdd:pfam05781 118 LMRNKNLVGLEAPEESETAEQERKESAAGEDVMSSIPdvLVKKVNFHQSLNT-----SANEKEVEAEFLRLSLAFKCDWF 192
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1134 TLEKRLRLEERSRDLAEENLKKEVKNCKGLLEKLAPLCEDDNQSLEIIQRLQKNFDVLVQSMSRVSNRSEMLGAIHQESR 1213
Cdd:pfam05781 193 TLEKRVKLEERSRDLAEENLKKEITNCLKLLESLTPLCEHDNQAQEIYKKLEKSIAVLSQCAARVASRAEMLGAINQESR 272
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1214 VSKAVEVMIQHVENLKRMYTKEHAELLELKETLVQSERSFGSYSERDDLRNKKTSGSQYSKPSS-RRVSVPAISRNIGNA 1292
Cdd:pfam05781 273 VSKAVEVMIQHVENLKRMYAKEHAELEELKQLLLQNSRSFNPLEDEDDCQIKKRSMSLNSKPSSlRRVSIASLPRNIGNS 352
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1293 SHFE-MPKLHEISEteadklcRTGNWRVMGMKQNSTRPTLQRFVSSCPWAESDEPSLMKGYEQESESPpaeekREEIVE- 1370
Cdd:pfam05781 353 GMASgMENNDRLSR-------RSSSWRILGNKQSEHRPSLHRFISTYSWSDAEEESCEVKAKDEEEPY-----GEEGVEk 420
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 1371 -RKSSLTEMGIKISSVLMtSTTCDQISSRFADFRHSVSKSNRGMWISVVLTVLFAAFIGLIASFAFQPSVDAAPVGTGDS 1449
Cdd:pfam05781 421 tRKPSLSEKKNNPSKWDV-SSIYETLASWLTNLYPSLRKANKVLWLSVAAIVLFAALMSFLTGQFFQSCVEAAPTQEGDS 499
|
410 420
....*....|....*....|..
gi 972982496 1450 WVAIQQFLWPYTGLRHNGQPPV 1471
Cdd:pfam05781 500 WCSLEHILWPFTGLQHEGPPPV 521
|
|
| KASH_CCD |
pfam14662 |
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of ... |
342-532 |
4.07e-66 |
|
Coiled-coil region of CCDC155 or KASH; This coiled-coil region is found in the central part of KASH or Klarsicht/ANC-1/Syne/homology proteins. KASH are a meiosis-specific proteins that localize at telomeres and interact with SUN1, thus being implicated in meiotic chromosome dynamics and homolog pairing.
Pssm-ID: 405365 [Multi-domain] Cd Length: 191 Bit Score: 221.59 E-value: 4.07e-66
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 342 LETSDLVYCVADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNME 421
Cdd:pfam14662 1 METSDLLTCVEDLQANNQKLLQENSKLKATVETREETNAKLLEENLNLRKQAKSQQQAVQKEKLLEEELEDLKLIVNSLE 80
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 422 ENRARSVAQNKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQI 501
Cdd:pfam14662 81 EARRSLLAQNKQLEKENQSLLQEIESLQEENKKNQAERDKLQKKKKELLKSKACLKEQLHSCEDLACNRETILIEKTTQI 160
|
170 180 190
....*....|....*....|....*....|.
gi 972982496 502 QELKSTIEEYSSVTDLLRAEKNKLESHVEML 532
Cdd:pfam14662 161 EELKSTVEEYSSIEEELRAEKSRLESQLPDM 191
|
|
| EF-hand_9 |
pfam14658 |
EF-hand domain; |
224-289 |
1.09e-17 |
|
EF-hand domain;
Pssm-ID: 405361 Cd Length: 66 Bit Score: 78.62 E-value: 1.09e-17
10 20 30 40 50 60
....*....|....*....|....*....|....*....|....*....|....*....|....*.
gi 972982496 224 DTIFHACDTQRRGKVSVSRIVDYLRHTTSRESEDSGLEELCNMLDPEHRDISIDLETYHAIMREWI 289
Cdd:pfam14658 1 ESTFEVCDTQKTGRVPVSRLIDYLRAVTGQDPQESRLQTLARELDPDGEDALVDLDTFLRVMRDWI 66
|
|
| SCP-1 |
pfam05483 |
Synaptonemal complex protein 1 (SCP-1); Synaptonemal complex protein 1 (SCP-1) is the major ... |
367-806 |
3.45e-07 |
|
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: 55.11 E-value: 3.45e-07
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 367 KLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNnmeenraRSVAQNKQMERENQSLISKIA 446
Cdd:pfam05483 255 KMKDLTFLLEESRDKANQLEEKTKLQDENLKELIEKKDHLTKELEDIKMSLQ-------RSMSTQKALEEDLQIATKTIC 327
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 447 SLQEENIKNMvdiDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKNKLE 526
Cdd:pfam05483 328 QLTEEKEAQM---EELNKAKAAHSFVVTEFEATTCSLEELLRTEQQRLEKNEDQLKIITMELQKKSSELEEMTKFKNNKE 404
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 527 SHVEMLQPALGLDGMSL---SGAYRLNQSTTGSLQtELALAQQAPETpaavsmlaapyhapldETLDRDVFLLLQGPASE 603
Cdd:pfam05483 405 VELEELKKILAEDEKLLdekKQFEKIAEELKGKEQ-ELIFLLQAREK----------------EIHDLEIQLTAIKTSEE 467
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 604 QNSAEFKAVVRKLHQDFREDICAVMCTLKRFTENHIESEDLREIWLKTMNSElEEKRNVWLQRVQLLDQYKcSLEEELIK 683
Cdd:pfam05483 468 HYLKEVEDLKTELEKEKLKNIELTAHCDKLLLENKELTQEASDMTLELKKHQ-EDIINCKKQEERMLKQIE-NLEEKEMN 545
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 684 VASRLRRCRTEVAHLKKELSARLPELEAQRQMQGDDKLRARPERGLAEaaSQTESSAPQVADKSTAASLLWEDESLLRND 763
Cdd:pfam05483 546 LRDELESVREEFIQKGDEVKCKLDKSEENARSIEYEVLKKEKQMKILE--NKCNNLKKQIENKNKNIEELHQENKALKKK 623
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 972982496 764 LQDTLRE-----------RVSLQDNSQALALSCGQFEQRLEEKRVNEHTAVEPV 806
Cdd:pfam05483 624 GSAENKQlnayeikvnklELELASAKQKFEEIIDNYQKEIEDKKISEEKLLEEV 677
|
|
| CCDC158 |
pfam15921 |
Coiled-coil domain-containing protein 158; CCDC158 is a family of proteins found in eukaryotes. ... |
351-558 |
5.28e-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: 51.27 E-value: 5.28e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLK-LAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVA 429
Cdd:pfam15921 319 LSDLESTVSQLRSELREAKrMYEDKIEELEKQLVLANSELTEARTERDQFSQESGNLDDQLQKLLADLHKREKELSLEKE 398
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 430 QNKQmerenqsliskiasLQEENIKNMVDIDHLQKkmaELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIE 509
Cdd:pfam15921 399 QNKR--------------LWDRDTGNSITIDHLRR---ELDDRNMEVQRLEALLKAMKSECQGQMERQMAAIQGKNESLE 461
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 972982496 510 EYSSVTDLLRAEKNKLESHVEMLQPalglDGMSLSGAYRLNQSTTGSLQ 558
Cdd:pfam15921 462 KVSSLTAQLESTKEMLRKVVEELTA----KKMTLESSERTVSDLTASLQ 506
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
361-536 |
8.69e-06 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 50.45 E-value: 8.69e-06
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 361 LQDEVRKLKLAVDtmeETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQS 440
Cdd:TIGR02169 693 LQSELRRIENRLD---ELSQELSDASRKIGEIEKEIEQLEQEEEKLKERLEELEEDLSSLEQEIENVKSELKELEARIEE 769
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 441 LISKIASLQEE--NIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKN----------AQIQELKSTI 508
Cdd:TIGR02169 770 LEEDLHKLEEAlnDLEARLSHSRIPEIQAELSKLEEEVSRIEARLREIEQKLNRLTLEKEylekeiqelqEQRIDLKEQI 849
|
170 180
....*....|....*....|....*...
gi 972982496 509 EEYSSVTDLLRAEKNKLESHVEMLQPAL 536
Cdd:TIGR02169 850 KSIEKEIENLNGKKEELEEELEELEAAL 877
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
327-570 |
2.21e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 49.28 E-value: 2.21e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 327 VGSLEAFGGEVSRGDLETSDLVYCVADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSgqqsamkeklL 406
Cdd:TIGR02168 231 VLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISR----------L 300
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 407 KGELEEMKVTLNNMEENRARSVAQNKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNI 486
Cdd:TIGR02168 301 EQQKQILRERLANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLEELEEQ 380
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 487 VGEKEALLCEKNAQIQELKSTIEEyssvtdlLRAEKNKLESHVEMLQPALGLDGMSLSGAYRLNQSTT-GSLQTELALAQ 565
Cdd:TIGR02168 381 LETLRSKVAQLELQIASLNNEIER-------LEARLERLEDRRERLQQEIEELLKKLEEAELKELQAElEELEEELEELQ 453
|
....*
gi 972982496 566 QAPET 570
Cdd:TIGR02168 454 EELER 458
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
359-532 |
3.45e-05 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 48.51 E-value: 3.45e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 359 QKLQDEVRKLKLA--VDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEE-------------N 423
Cdd:TIGR02168 216 KELKAELRELELAllVLRLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEeieelqkelyalaN 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 424 RARSVAQNKQMEREN-QSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQ 502
Cdd:TIGR02168 296 EISRLEQQKQILRERlANLERQLEELEAQLEELESKLDELAEELAELEEKLEELKEELESLEAELEELEAELEELESRLE 375
|
170 180 190
....*....|....*....|....*....|
gi 972982496 503 ELKSTIEEYSSVTDLLRAEKNKLESHVEML 532
Cdd:TIGR02168 376 ELEEQLETLRSKVAQLELQIASLNNEIERL 405
|
|
| COG4372 |
COG4372 |
Uncharacterized protein, contains DUF3084 domain [Function unknown]; |
352-561 |
4.07e-05 |
|
Uncharacterized protein, contains DUF3084 domain [Function unknown];
Pssm-ID: 443500 [Multi-domain] Cd Length: 370 Bit Score: 47.59 E-value: 4.07e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 352 ADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELktQAKSGQQSAMKEKL--LKGELEEMKVTLNNMEENRARSVA 429
Cdd:COG4372 52 EELEQAREELEQLEEELEQARSELEQLEEELEELNEQL--QAAQAELAQAQEELesLQEEAEELQEELEELQKERQDLEQ 129
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 430 QNKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELcavnaDLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIE 509
Cdd:COG4372 130 QRKQLEAQIAELQSEIAEREEELKELEEQLESLQEELAAL-----EQELQALSEAEAEQALDELLKEANRNAEKEEELAE 204
|
170 180 190 200 210
....*....|....*....|....*....|....*....|....*....|..
gi 972982496 510 EYSSVTDLLRAEKNKLESHVEMLQPALGLDGMSLSGAYRLNQSTTGSLQTEL 561
Cdd:COG4372 205 AEKLIESLPRELAEELLEAKDSLEAKLGLALSALLDALELEEDKEELLEEVI 256
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
353-527 |
4.12e-05 |
|
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of Mycoplasma species. Members average 750 amino acids in length, including signal peptide. Sequences are predicted (Jpred 3) to be almost entirely alpha-helical. These sequences show strong periodicity (consistent with long alpha helical structures) and low complexity rich in D,E,N,Q, and K. Genes encoding these proteins are often found in tandem. The function is unknown.
Pssm-ID: 275316 [Multi-domain] Cd Length: 745 Bit Score: 48.09 E-value: 4.12e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 353 DLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKS----GQQSAMKEKLLKGELEEMKVTLNNMEENRARSV 428
Cdd:TIGR04523 353 NSESENSEKQRELEEKQNEIEKLKKENQSYKQEIKNLESQINDleskIQNQEKLNQQKDEQIKKLQQEKELLEKEIERLK 432
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 429 AQNKQMERENQSLISKIASLqEENIKNMVD-IDHLQKKMAELCA----VNADLQMQVHSLDNIVGEKEALLCEK---NAQ 500
Cdd:TIGR04523 433 ETIIKNNSEIKDLTNQDSVK-ELIIKNLDNtRESLETQLKVLSRsinkIKQNLEQKQKELKSKEKELKKLNEEKkelEEK 511
|
170 180
....*....|....*....|....*..
gi 972982496 501 IQELKSTIEEYSSVTDLLRAEKNKLES 527
Cdd:TIGR04523 512 VKDLTKKISSLKEKIEKLESEKKEKES 538
|
|
| Taxilin |
pfam09728 |
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain ... |
354-530 |
5.48e-05 |
|
Myosin-like coiled-coil protein; Taxilin contains an extraordinarily long coiled-coil domain in its C-terminal half and is ubiquitously expressed. It is a novel binding partner of several syntaxin family members and is possibly involved in Ca2+-dependent exocytosis in neuroendocrine cells. Gamma-taxilin, described as leucine zipper protein Factor Inhibiting ATF4-mediated Transcription (FIAT), localizes to the nucleus in osteoblasts and dimerizes with ATF4 to form inactive dimers, thus inhibiting ATF4-mediated transcription.
Pssm-ID: 462861 [Multi-domain] Cd Length: 302 Bit Score: 46.87 E-value: 5.48e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 354 LQFNNQKLQDEVRKLKLAVDTMEE-------TNNKLMEENEELKTQAKSgQQSAMKEKlLKGELEEMKVTlnnMEENRAR 426
Cdd:pfam09728 51 LQKEKDQLQSELSKAILAKSKLEKlcrelqkQNKKLKEESKKLAKEEEE-KRKELSEK-FQSTLKDIQDK---MEEKSEK 125
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 427 svaqNKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMaelcavnaDLQMQVHS--LDNIVGEKEALLCEK-NAQIQE 503
Cdd:pfam09728 126 ----NNKLREENEELREKLKSLIEQYELRELHFEKLLKTK--------ELEVQLAEakLQQATEEEEKKAQEKeVAKARE 193
|
170 180
....*....|....*....|....*..
gi 972982496 504 LKSTIEEYSSVTDLLRaekNKLESHVE 530
Cdd:pfam09728 194 LKAQVQTLSETEKELR---EQLNLYVE 217
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
343-530 |
6.30e-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: 6.30e-05
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 343 ETSDLVYCVADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQ----QSAMKEKLLKGELEEMKVTLN 418
Cdd:TIGR04523 219 QISELKKQNNQLKDNIEKKQQEINEKTTEISNTQTQLNQLKDEQNKIKKQLSEKQkeleQNNKKIKELEKQLNQLKSEIS 298
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 419 NMeenrarsvaqNKQMERE-NQSLISKIASLQE--ENIKNmvDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLC 495
Cdd:TIGR04523 299 DL----------NNQKEQDwNKELKSELKNQEKklEEIQN--QISQNNKIISQLNEQISQLKKELTNSESENSEKQRELE 366
|
170 180 190
....*....|....*....|....*....|....*
gi 972982496 496 EKNAQIQELKSTIEEYSSVTDLLRAEKNKLESHVE 530
Cdd:TIGR04523 367 EKQNEIEKLKKENQSYKQEIKNLESQINDLESKIQ 401
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
458-775 |
1.18e-04 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 46.97 E-value: 1.18e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 458 DIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKNKLESHVEMLQpalg 537
Cdd:TIGR02168 233 RLEELREELEELQEELKEAEEELEELTAELQELEEKLEELRLEVSELEEEIEELQKELYALANEISRLEQQKQILR---- 308
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 538 ldgmslsgaYRLNQSTTGSLQTELALAQqapetpaavsmlaapyhapLDETLDRDVFLLlqgpasEQNSAEFkAVVRKLH 617
Cdd:TIGR02168 309 ---------ERLANLERQLEELEAQLEE-------------------LESKLDELAEEL------AELEEKL-EELKEEL 353
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 618 QDFREdicavmctlkRFTENHIESEDLREIWlktmnselEEKRNVWLQRVQLLDQykcsLEEELIKVASRLRRCRTEVAH 697
Cdd:TIGR02168 354 ESLEA----------ELEELEAELEELESRL--------EELEEQLETLRSKVAQ----LELQIASLNNEIERLEARLER 411
|
250 260 270 280 290 300 310
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*...
gi 972982496 698 LKKELSARLPELEAQRQmQGDDKLRARPERGLAEAASQTESSAPQVADKSTAASLLWEDESLLRNDLQDTLRERVSLQ 775
Cdd:TIGR02168 412 LEDRRERLQQEIEELLK-KLEEAELKELQAELEELEEELEELQEELERLEEALEELREELEEAEQALDAAERELAQLQ 488
|
|
| YhaN |
COG4717 |
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown]; |
363-782 |
1.21e-04 |
|
Uncharacterized conserved protein YhaN, contains AAA domain [Function unknown];
Pssm-ID: 443752 [Multi-domain] Cd Length: 641 Bit Score: 46.68 E-value: 1.21e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 363 DEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNmeenrARSVAQNKQMERENQSLI 442
Cdd:COG4717 71 KELKELEEELKEAEEKEEEYAELQEELEELEEELEELEAELEELREELEKLEKLLQL-----LPLYQELEALEAELAELP 145
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 443 SKIASLQEEniknMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVG-EKEALLCEKNAQIQELKSTIEEYSSVTDLLRAE 521
Cdd:COG4717 146 ERLEELEER----LEELRELEEELEELEAELAELQEELEELLEQLSlATEEELQDLAEELEELQQRLAELEEELEEAQEE 221
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 522 KNKLESHVEMLQPALGLDGM--SLSGAYRLNQSTTG--SLQTELALAQQAPETPAAVSMLAAPYHAPLDETLDRDVFLLL 597
Cdd:COG4717 222 LEELEEELEQLENELEAAALeeRLKEARLLLLIAAAllALLGLGGSLLSLILTIAGVLFLVLGLLALLFLLLAREKASLG 301
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 598 QGPASEQNSAEFKAVVRKLHQDFREDIcavmcTLKRFTENHIESEDLREIW-LKTMNSELEEKRNVWL------QRVQLL 670
Cdd:COG4717 302 KEAEELQALPALEELEEEELEELLAAL-----GLPPDLSPEELLELLDRIEeLQELLREAEELEEELQleeleqEIAALL 376
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 671 DQYKCSLEEELIKVASRLRRC---RTEVAHLKKELSARLPELEAQRQMQGDDKLRARpergLAEAASQTESSAPQVADKS 747
Cdd:COG4717 377 AEAGVEDEEELRAALEQAEEYqelKEELEELEEQLEELLGELEELLEALDEEELEEE----LEELEEELEELEEELEELR 452
|
410 420 430
....*....|....*....|....*....|....*..
gi 972982496 748 TA-ASLLWEDESLLRND-LQDTLRERVSLQDNSQALA 782
Cdd:COG4717 453 EElAELEAELEQLEEDGeLAELLQELEELKAELRELA 489
|
|
| Leu_zip |
pfam15294 |
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 ... |
351-506 |
1.25e-04 |
|
Leucine zipper; This family includes Leucine zipper transcription factor-like protein 1 (LZTFL1) and Leucine zipper protein 2 (LUZP2).
Pssm-ID: 464620 [Multi-domain] Cd Length: 276 Bit Score: 45.47 E-value: 1.25e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEmkvtLNNMEENRArsvaq 430
Cdd:pfam15294 128 SALLHMEIERLKEENEKLKERLKTLESQATQALDEKSKLEKALKDLQKEQGAKKDVKSNLKE----ISDLEEKMA----- 198
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 431 nkQMERENQSLISKIASLQEENIKNMVDIDHlqkkmaELCAVNADLQMQVHSLDNIVGEKEA------LLCEKNAQIQEL 504
Cdd:pfam15294 199 --ALKSDLEKTLNASTALQKSLEEDLASTKH------ELLKVQEQLEMAEKELEKKFQQTAAyrnmkeMLTKKNEQIKEL 270
|
..
gi 972982496 505 KS 506
Cdd:pfam15294 271 RK 272
|
|
| UPF0242 |
pfam06785 |
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal ... |
359-459 |
2.06e-04 |
|
Uncharacterized protein family (UPF0242) N-terminus; This region includes an N-terminal transmembrane region and a C-terminal coiled-coil.
Pssm-ID: 429117 [Multi-domain] Cd Length: 194 Bit Score: 44.04 E-value: 2.06e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 359 QKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKL-LKGELEEMKVTLNNMEEN--RARSVAQNKQME 435
Cdd:pfam06785 93 EELQSEEERLEEELSQKEEELRRLTEENQQLQIQLQQISQDFAEFRLeSEEQLAEKQLLINEYQQTieEQRSVLEKRQDQ 172
|
90 100
....*....|....*....|....
gi 972982496 436 RENqsLISKIASLQEEnIKNMVDI 459
Cdd:pfam06785 173 IEN--LESKVRDLNYE-IKTLLQL 193
|
|
| CwlO1 |
COG3883 |
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function ... |
351-580 |
2.66e-04 |
|
Uncharacterized N-terminal coiled-coil domain of peptidoglycan hydrolase CwlO [Function unknown];
Pssm-ID: 443091 [Multi-domain] Cd Length: 379 Bit Score: 45.21 E-value: 2.66e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKeklLKGELEEMKVTLnnmeENRARSVAQ 430
Cdd:COG3883 25 LSELQAELEAAQAELDALQAELEELNEEYNELQAELEALQAEIDKLQAEIAE---AEAEIEERREEL----GERARALYR 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 431 NKQ--------MEREN-QSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQI 501
Cdd:COG3883 98 SGGsvsyldvlLGSESfSDFLDRLSALSKIADADADLLEELKADKAELEAKKAELEAKLAELEALKAELEAAKAELEAQQ 177
|
170 180 190 200 210 220 230
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....
gi 972982496 502 QELKSTIEEYSSVTDLLRAEKNKLESHVEMLQPALGLDGMSLSGAYRLNQSTTGSLQTELALAQQAPETPAAVSMLAAP 580
Cdd:COG3883 178 AEQEALLAQLSAEEAAAEAQLAELEAELAAAEAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAAASAAGAGAAGAAG 256
|
|
| CBD_MYO6-like |
cd21759 |
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, ... |
401-480 |
3.78e-04 |
|
calmodulin binding domain found in unconventional myosin-VI and similar proteins; Myosins, which are actin-based motor molecules with ATPase activity, include unconventional myosins that serve in intracellular movements. Myosin-VI, also called unconventional myosin-6 (MYO6), is a reverse-direction motor protein that moves towards the minus-end of actin filaments. It is required for the structural integrity of the Golgi apparatus via the p53-dependent pro-survival pathway. Myosin-VI appears to be involved in a very early step of clathrin-mediated endocytosis in polarized epithelial cells. It modulates RNA polymerase II-dependent transcription. As part of the DISP (DOCK7-Induced Septin disPlacement) complex, Myosin-VI may regulate the association of septins with actin and thereby regulate the actin cytoskeleton. Myosin-VI is encoded by gene MYO6, the human homolog of the gene responsible for deafness in Snell's waltzer mice. It is mutated in autosomal dominant non-syndromic hearing loss. This family also includes Drosophila melanogaster unconventional myosin VI Jaguar (Jar; also called myosin heavy chain 95F (Mhc95F), or 95F MHC), which is a motor protein necessary for the morphogenesis of epithelial tissues during Drosophila development. Jar is required for basal protein targeting and correct spindle orientation in mitotic neuroblasts. It contributes to synaptic transmission and development at the Drosophila neuromuscular junction. Together with CLIP-190 (CAP-Gly domain-containing/cytoplasmic linker protein 190), Jar may coordinate the interaction between the actin and microtubule cytoskeleton. Jar may link endocytic vesicles to microtubules and possibly be involved in transport in the early embryo and in the dynamic process of dorsal closure; its function is believed to change during the life cycle. This model corresponds to the calmodulin (CaM) binding domain (CBD), which consists of three subdomains: a unique insert (Insert 2 or Ins2), an IQ motif, and a proximal tail domain (PTD, also known as lever arm extension or LAE).
Pssm-ID: 409646 [Multi-domain] Cd Length: 149 Bit Score: 42.49 E-value: 3.78e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 401 MKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQSLISKI---ASLQEENIKNMVdiDHLQKKMAELcavNADLQ 477
Cdd:cd21759 72 RKIRALEKQLKEMEEIASQLKKDKDKWTKQVKELKKEIDALIKKIktnDMITRKEIDKLY--NALVKKVDKQ---LAELQ 146
|
...
gi 972982496 478 MQV 480
Cdd:cd21759 147 KKL 149
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
351-533 |
5.15e-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: 5.15e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLKlavDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQ 430
Cdd:TIGR02168 700 LAELRKELEELEEELEQLR---KELEELSRQISALRKDLARLEAEVEQLEERIAQLSKELTELEAEIEELEERLEEAEEE 776
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 431 NKQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEE 510
Cdd:TIGR02168 777 LAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIAATERRLEDLEEQIEELSEDIES 856
|
170 180
....*....|....*....|...
gi 972982496 511 YSSVTDLLRAEKNKLESHVEMLQ 533
Cdd:TIGR02168 857 LAAEIEELEELIEELESELEALL 879
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-533 |
5.74e-04 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 44.54 E-value: 5.74e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 352 ADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQN 431
Cdd:COG1196 239 AELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLAELARLEQDIARLEERRRELEERL 318
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 432 KQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEY 511
Cdd:COG1196 319 EELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEELEELAEELLEALRAAAEL 398
|
170 180
....*....|....*....|...
gi 972982496 512 -SSVTDLLRAEKNKLESHVEMLQ 533
Cdd:COG1196 399 aAQLEELEEAEEALLERLERLEE 421
|
|
| PspA_IM30 |
pfam04012 |
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent ... |
389-548 |
9.41e-04 |
|
PspA/IM30 family; This family includes PspA a protein that suppresses sigma54-dependent transcription. The PspA protein, a negative regulator of the Escherichia coli phage shock psp operon, is produced when virulence factors are exported through secretins in many Gram-negative pathogenic bacteria and its homolog in plants, VIPP1, plays a critical role in thylakoid biogenesis, essential for photosynthesis. Activation of transcription by the enhancer-dependent bacterial sigma(54) containing RNA polymerase occurs through ATP hydrolysis-driven protein conformational changes enabled by activator proteins that belong to the large AAA(+) mechanochemical protein family. It has been shown that PspA directly and specifically acts upon and binds to the AAA(+) domain of the PspF transcription activator.
Pssm-ID: 461130 [Multi-domain] Cd Length: 215 Bit Score: 42.36 E-value: 9.41e-04
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 389 LKTQAKSGQQSAMK-EKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQSLISKIASLQEENIKNMvdidhlqKKMA 467
Cdd:pfam04012 9 VRANIHEGLDKAEDpEKMLEQAIRDMQSELVKARQALAQTIARQKQLERRLEQQTEQAKKLEEKAQAAL-------TKGN 81
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 468 ELCAVNADLQMQvhSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKNKLES------HVEMLQPALGldGM 541
Cdd:pfam04012 82 EELAREALAEKK--SLEKQAEALETQLAQQRSAVEQLRKQLAALETKIQQLKAKKNLLKArlkaakAQEAVQTSLG--SL 157
|
....*..
gi 972982496 542 SLSGAYR 548
Cdd:pfam04012 158 STSSATD 164
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
357-533 |
1.20e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.20e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 357 NNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRArsvAQNKQMER 436
Cdd:COG4942 25 AEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIA---ELRAELEA 101
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 437 ENQSLISKIASLQEENIKNMVDI---------------------DHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLC 495
Cdd:COG4942 102 QKEELAELLRALYRLGRQPPLALllspedfldavrrlqylkylaPARREQAEELRADLAELAALRAELEAERAELEALLA 181
|
170 180 190
....*....|....*....|....*....|....*...
gi 972982496 496 EKNAQIQELKSTIEEYSSVTDLLRAEKNKLESHVEMLQ 533
Cdd:COG4942 182 ELEEERAALEALKAERQKLLARLEKELAELAAELAELQ 219
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
371-567 |
1.27e-03 |
|
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 443969 [Multi-domain] Cd Length: 377 Bit Score: 42.83 E-value: 1.27e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 371 AVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQSLISKIASLQE 450
Cdd:COG4942 18 QADAAAEAEAELEQLQQEIAELEKELAALKKEEKALLKQLAALERRIAALARRIRALEQELAALEAELAELEKEIAELRA 97
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 451 EniknmvdIDHLQKKMAELcAVNADLQMQVHSLDNIVGEK------------EALLCEKNAQIQELKSTIEEYSSVTDLL 518
Cdd:COG4942 98 E-------LEAQKEELAEL-LRALYRLGRQPPLALLLSPEdfldavrrlqylKYLAPARREQAEELRADLAELAALRAEL 169
|
170 180 190 200
....*....|....*....|....*....|....*....|....*....
gi 972982496 519 RAEKNKLESHVEMLQPALGldgmSLSGAYRLNQSTTGSLQTELALAQQA 567
Cdd:COG4942 170 EAERAELEALLAELEEERA----ALEALKAERQKLLARLEKELAELAAE 214
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
376-731 |
1.44e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 43.51 E-value: 1.44e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 376 EETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQSLISKIASLQEENIKN 455
Cdd:TIGR02168 666 AKTNSSILERRREIEELEEKIEELEEKIAELEKALAELRKELEELEEELEQLRKELEELSRQISALRKDLARLEAEVEQL 745
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 456 MVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKNkleshvemlqpa 535
Cdd:TIGR02168 746 EERIAQLSKELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELT------------ 813
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 536 lgldgmSLSGAYRLNQSTTGSLQTELALAQQAPETpaavsmlaapyhapLDETLDRdvfLLLQGPASEQNSAEFKAVVRK 615
Cdd:TIGR02168 814 ------LLNEEAANLRERLESLERRIAATERRLED--------------LEEQIEE---LSEDIESLAAEIEELEELIEE 870
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 616 LHQDfredicavmctLKRFTENHIESEDLREIwLKTMNSELEEKRNVWLQRVQLLDQYKCSLEEELIKVASRLRRCRTEV 695
Cdd:TIGR02168 871 LESE-----------LEALLNERASLEEALAL-LRSELEELSEELRELESKRSELRRELEELREKLAQLELRLEGLEVRI 938
|
330 340 350
....*....|....*....|....*....|....*...
gi 972982496 696 AHLKKELSA--RLPELEAQRQMQGDDKLRARPERGLAE 731
Cdd:TIGR02168 939 DNLQERLSEeySLTLEEAEALENKIEDDEEEARRRLKR 976
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-809 |
1.61e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 43.00 E-value: 1.61e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 352 ADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQN 431
Cdd:COG1196 302 QDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAELAEAEEEL 381
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 432 KQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEY 511
Cdd:COG1196 382 EELAEELLEALRAAAELAAQLEELEEAEEALLERLERLEEELEELEEALAELEEEEEEEEEALEEAAEEEAELEEEEEAL 461
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 512 SSVTDLLRAEKNKLESHVEMLQPALGLDGMSLSGAYRLNQSTTGSLQT--ELALAQQAPETPAAVSMLAAPYHAPLDETL 589
Cdd:COG1196 462 LELLAELLEEAALLEAALAELLEELAEAAARLLLLLEAEADYEGFLEGvkAALLLAGLRGLAGAVAVLIGVEAAYEAALE 541
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 590 DRDVFLLLQGPASEQNSAEFKAVVRKLHQDFREDI--CAVMCTLKRFTENHIESEDLREIWLKTMNSELEEKRNVWLQRV 667
Cdd:COG1196 542 AALAAALQNIVVEDDEVAAAAIEYLKAAKAGRATFlpLDKIRARAALAAALARGAIGAAVDLVASDLREADARYYVLGDT 621
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 668 QLLDQYKCSLEEELIKVASRLRRCRTEVAHLKKELSARLPELEAQRQMQGDDKLRARPERGLAEAASQTESSAPQVADKS 747
Cdd:COG1196 622 LLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEELAERLAEEELELEEALLA 701
|
410 420 430 440 450 460
....*....|....*....|....*....|....*....|....*....|....*....|..
gi 972982496 748 TAASLLWEDESLLRNDLQDTLRERVSLQDNSQALAlscgQFEQRLEEKRVNEHTAVEPVPDL 809
Cdd:COG1196 702 EEEEERELAEAEEERLEEELEEEALEEQLEAEREE----LLEELLEEEELLEEEALEELPEP 759
|
|
| SMC_prok_A |
TIGR02169 |
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of ... |
302-593 |
2.15e-03 |
|
chromosome segregation protein SMC, primarily archaeal type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. It is found in a single copy and is homodimeric in prokaryotes, but six paralogs (excluded from this family) are found in eukarotes, where SMC proteins are heterodimeric. This family represents the SMC protein of archaea and a few bacteria (Aquifex, Synechocystis, etc); the SMC of other bacteria is described by TIGR02168. The N- and C-terminal domains of this protein are well conserved, but the central hinge region is skewed in composition and highly divergent. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274009 [Multi-domain] Cd Length: 1164 Bit Score: 42.75 E-value: 2.15e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 302 EGETEDSQKLSDSLSARKSFAMNMTVGSLEAFGGEVSRGDLETSDLVYCVADLQFnnqKLQDEVRKLKLAVDTMEETNNK 381
Cdd:TIGR02169 204 RREREKAERYQALLKEKREYEGYELLKEKEALERQKEAIERQLASLEEELEKLTE---EISELEKRLEEIEQLLEELNKK 280
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 382 LME--ENEELKTQAKSGQQSAMKEKL------LKGELEEMKVTLNNMEENRARSVAQNKQMERENQ-------SLISKIA 446
Cdd:TIGR02169 281 IKDlgEEEQLRVKEKIGELEAEIASLersiaeKERELEDAEERLAKLEAEIDKLLAEIEELEREIEeerkrrdKLTEEYA 360
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 447 SLQEENIKNMVDIDHLQKKMAELCAVNADLQ----MQVHSLDNIVGEKEALLCEK----------NAQIQELKSTIEEYS 512
Cdd:TIGR02169 361 ELKEELEDLRAELEEVDKEFAETRDELKDYRekleKLKREINELKRELDRLQEELqrlseeladlNAAIAGIEAKINELE 440
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 513 SVTDLLRAEKNKLESHVEMLQPALGldgmSLSGAYRLNQSTTGSLQTELALAQQ---APETPAAVSMLAAPYHAPLDETL 589
Cdd:TIGR02169 441 EEKEDKALEIKKQEWKLEQLAADLS----KYEQELYDLKEEYDRVEKELSKLQRelaEAEAQARASEERVRGGRAVEEVL 516
|
....
gi 972982496 590 DRDV 593
Cdd:TIGR02169 517 KASI 520
|
|
| Mplasa_alph_rch |
TIGR04523 |
helix-rich Mycoplasma protein; Members of this family occur strictly within a subset of ... |
353-527 |
2.25e-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: 42.70 E-value: 2.25e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 353 DLQFNNQKLQDEVRKLKLavdTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEenrarsvAQNK 432
Cdd:TIGR04523 465 SLETQLKVLSRSINKIKQ---NLEQKQKELKSKEKELKKLNEEKKELEEKVKDLTKKISSLKEKIEKLE-------SEKK 534
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 433 QMERENQSLISKIASLQEENIKNMVD--IDHLQKKMAELCAVNAdlqmqvhSLDNIVGEKEALLCEKNAQIQELKSTIEE 510
Cdd:TIGR04523 535 EKESKISDLEDELNKDDFELKKENLEkeIDEKNKEIEELKQTQK-------SLKKKQEEKQELIDQKEKEKKDLIKEIEE 607
|
170 180
....*....|....*....|....
gi 972982496 511 Y----SSVTD---LLRAEKNKLES 527
Cdd:TIGR04523 608 KekkiSSLEKeleKAKKENEKLSS 631
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
359-533 |
2.65e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 42.23 E-value: 2.65e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 359 QKLQDE--VRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMER 436
Cdd:COG1196 216 RELKEElkELEAELLLLKLRELEAELEELEAELEELEAELEELEAELAELEAELEELRLELEELELELEEAQAEEYELLA 295
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 437 ENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSS-VT 515
Cdd:COG1196 296 ELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEALLEAEAeLA 375
|
170
....*....|....*...
gi 972982496 516 DLLRAEKNKLESHVEMLQ 533
Cdd:COG1196 376 EAEEELEELAEELLEALR 393
|
|
| SMC_prok_B |
TIGR02168 |
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of ... |
364-533 |
2.84e-03 |
|
chromosome segregation protein SMC, common bacterial type; SMC (structural maintenance of chromosomes) proteins bind DNA and act in organizing and segregating chromosomes for partition. SMC proteins are found in bacteria, archaea, and eukaryotes. This family represents the SMC protein of most bacteria. The smc gene is often associated with scpB (TIGR00281) and scpA genes, where scp stands for segregation and condensation protein. SMC was shown (in Caulobacter crescentus) to be induced early in S phase but present and bound to DNA throughout the cell cycle. [Cellular processes, Cell division, DNA metabolism, Chromosome-associated proteins]
Pssm-ID: 274008 [Multi-domain] Cd Length: 1179 Bit Score: 42.35 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 364 EVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQsamKEKLLKGELEEMKVTLNNMEENRARSVAQNKQMERENQSLIS 443
Cdd:TIGR02168 678 EIEELEEKIEELEEKIAELEKALAELRKELEELEE---ELEQLRKELEELSRQISALRKDLARLEAEVEQLEERIAQLSK 754
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 444 KIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSVTDLLRAEKN 523
Cdd:TIGR02168 755 ELTELEAEIEELEERLEEAEEELAEAEAEIEELEAQIEQLKEELKALREALDELRAELTLLNEEAANLRERLESLERRIA 834
|
170
....*....|
gi 972982496 524 KLESHVEMLQ 533
Cdd:TIGR02168 835 ATERRLEDLE 844
|
|
| Cast |
pfam10174 |
RIM-binding protein of the cytomatrix active zone; This is a family of proteins that form part ... |
351-564 |
2.84e-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: 42.12 E-value: 2.84e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLKLAVDTMEEtnnklmEENEELKtqaksgQQSAMKE--KLLKGELEEMKVTLNnmeenrarsv 428
Cdd:pfam10174 242 ISSLERNIRDLEDEVQMLKTNGLLHTE------DREEEIK------QMEVYKShsKFMKNKIDQLKQELS---------- 299
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 429 aqnkQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQEL---K 505
Cdd:pfam10174 300 ----KKESELLALQTKLETLTNQNSDCKQHIEVLKESLTAKEQRAAILQTEVDALRLRLEEKESFLNKKTKQLQDLteeK 375
|
170 180 190 200 210 220
....*....|....*....|....*....|....*....|....*....|....*....|....
gi 972982496 506 STIE-EYSSVTDLLRAEKNK---LESHVEMLQPALGLDGMSLSGAYRLNQS-TTGSLQTELALA 564
Cdd:pfam10174 376 STLAgEIRDLKDMLDVKERKinvLQKKIENLQEQLRDKDKQLAGLKERVKSlQTDSSNTDTALT 439
|
|
| PRK03918 |
PRK03918 |
DNA double-strand break repair ATPase Rad50; |
351-536 |
5.63e-03 |
|
DNA double-strand break repair ATPase Rad50;
Pssm-ID: 235175 [Multi-domain] Cd Length: 880 Bit Score: 41.20 E-value: 5.63e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 351 VADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAK---SGQQSAMKEKLLKGELEEMKVTLNNMEENRARS 427
Cdd:PRK03918 240 IEELEKELESLEGSKRKLEEKIRELEERIEELKKEIEELEEKVKelkELKEKAEEYIKLSEFYEEYLDELREIEKRLSRL 319
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 428 VAQNKQMERENQSLISKIASLQEenIKNmvDIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEK----NAQIQE 503
Cdd:PRK03918 320 EEEINGIEERIKELEEKEERLEE--LKK--KLKELEKRLEELEERHELYEEAKAKKEELERLKKRLTGLTpeklEKELEE 395
|
170 180 190
....*....|....*....|....*....|...
gi 972982496 504 LKSTIEEYSSVTDLLRAEKNKLESHVEMLQPAL 536
Cdd:PRK03918 396 LEKAKEEIEEEISKITARIGELKKEIKELKKAI 428
|
|
| Smc |
COG1196 |
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning]; ... |
352-799 |
6.79e-03 |
|
Chromosome segregation ATPase Smc [Cell cycle control, cell division, chromosome partitioning];
Pssm-ID: 440809 [Multi-domain] Cd Length: 983 Bit Score: 41.08 E-value: 6.79e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 352 ADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEKLLKGELEEMKVTLNNMEENRARSVAQN 431
Cdd:COG1196 288 AEEYELLAELARLEQDIARLEERRRELEERLEELEEELAELEEELEELEEELEELEEELEEAEEELEEAEAELAEAEEAL 367
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 432 KQMERENQSLISKIASLQEENIKNMVDIDHLQKKMAELCAVNADLQMQVHSL-DNIVGEKEALLCEKNAQIQELKSTIEE 510
Cdd:COG1196 368 LEAEAELAEAEEELEELAEELLEALRAAAELAAQLEELEEAEEALLERLERLeEELEELEEALAELEEEEEEEEEALEEA 447
|
170 180 190 200 210 220 230 240
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 511 YSSVTDLLRAEKNKLESHVEMLQPALGLDgmslSGAYRLNQSTTGSLQTELALAQQAPETPAAVSMLAAPYHAPLDETLD 590
Cdd:COG1196 448 AEEEAELEEEEEALLELLAELLEEAALLE----AALAELLEELAEAAARLLLLLEAEADYEGFLEGVKAALLLAGLRGLA 523
|
250 260 270 280 290 300 310 320
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 591 RDVFLLLQGPASEQNSAEFKAVVRKLHQDFREDICAVMC--TLKRFTENHIESEDLREIWLKTMNSELEEKRNVWLQRVQ 668
Cdd:COG1196 524 GAVAVLIGVEAAYEAALEAALAAALQNIVVEDDEVAAAAieYLKAAKAGRATFLPLDKIRARAALAAALARGAIGAAVDL 603
|
330 340 350 360 370 380 390 400
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 669 L-LDQYKCSLEEELIKVASRLRRCRTEVAHLKKELSARLPELEAQRQMQGDDKLRARPERGLAEAASQTESSAPQVADKS 747
Cdd:COG1196 604 VaSDLREADARYYVLGDTLLGRTLVAARLEAALRRAVTLAGRLREVTLEGEGGSAGGSLTGGSRRELLAALLEAEAELEE 683
|
410 420 430 440 450
....*....|....*....|....*....|....*....|....*....|....
gi 972982496 748 TAASLLWEDESLLRNDLQDTLRERVSLQDNSQA--LALSCGQFEQRLEEKRVNE 799
Cdd:COG1196 684 LAERLAEEELELEEALLAEEEEERELAEAEEERleEELEEEALEEQLEAEREEL 737
|
|
| TACC_C |
pfam05010 |
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a ... |
330-504 |
7.88e-03 |
|
Transforming acidic coiled-coil-containing protein (TACC), C-terminal; This entry represents a C-terminal domain found in the the proteins TACC 1, 2 and 3 (TACC1-3). TACC1 is found concentrated in the centrosomes of eukaryotes which may play a conserved role in organizing centrosomal microtubules. The human TACC proteins have been linked to cancer and TACC2 has been identified as a possible tumour suppressor (AZU-1). TACC 3 from Xenopus laevis, also known as maskin, associates XMAP215 and promotes efficient microtubule elongation during mitosis. Maskin is also found to bind CPEB and elF-4E. Interestingly, the functional homolog (Alp7) in Schizosaccharomyces pombe (not included in this entry) has been shown to be required for organization of bipolar spindles.
Pssm-ID: 461517 [Multi-domain] Cd Length: 201 Bit Score: 39.27 E-value: 7.88e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 330 LEAFGGEVSRGDLEtsdlvycVADLQFNNQKLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSGQQSAMKEK-LLKG 408
Cdd:pfam05010 10 LEKARNEIEEKELE-------INELKAKYEELRRENLEMRKIVAEFEKTIAQMIEEKQKQKELEHAEIQKVLEEKdQALA 82
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 409 EL--------------EEMKVTLNNMEENRA--RSVAQN-----KQMERENQSLisKIASLQEENIKNmVDIDHLQKKM- 466
Cdd:pfam05010 83 DLnsveksfsdlfkryEKQKEVISGYKKNEEslKKCAQDylariKKEEQRYQAL--KAHAEEKLDQAN-EEIAQVRSKAk 159
|
170 180 190 200
....*....|....*....|....*....|....*....|.
gi 972982496 467 AELCAVNADL---QMQVHSLdnivgekEALLCEKNAQIQEL 504
Cdd:pfam05010 160 AETAALQASLrkeQMKVQSL-------ERQLEQKTKENEEL 193
|
|
| EnvC |
COG4942 |
Septal ring factor EnvC, activator of murein hydrolases AmiA and AmiB [Cell cycle control, ... |
360-526 |
8.92e-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: 40.13 E-value: 8.92e-03
10 20 30 40 50 60 70 80
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 360 KLQDEVRKLKLAVDTMEETNNKLMEENEELKTQAKSgQQSAMKEKLLK----GELEEMKVTLNNMEENRA-RSVAQNKQM 434
Cdd:COG4942 66 ALARRIRALEQELAALEAELAELEKEIAELRAELEA-QKEELAELLRAlyrlGRQPPLALLLSPEDFLDAvRRLQYLKYL 144
|
90 100 110 120 130 140 150 160
....*....|....*....|....*....|....*....|....*....|....*....|....*....|....*....|
gi 972982496 435 ERENQSLISKIASLQEENIKNmvdIDHLQKKMAELCAVNADLQMQVHSLDNIVGEKEALLCEKNAQIQELKSTIEEYSSV 514
Cdd:COG4942 145 APARREQAEELRADLAELAAL---RAELEAERAELEALLAELEEERAALEALKAERQKLLARLEKELAELAAELAELQQE 221
|
170
....*....|..
gi 972982496 515 TDLLRAEKNKLE 526
Cdd:COG4942 222 AEELEALIARLE 233
|
|
| |
